Artykuły w czasopismach: „Phosphoproteins”

1

Qiao, Yuting, Xianrong Liu, Zhi Jia, Peng Zhang, Li Gao, Bingxin Liu, Lijuan Qiao i Lei Zhang. "In Situ Growth Intercalation Structure MXene@Anatase/Rutile TiO2 Ternary Heterojunction with Excellent Phosphoprotein Detection in Sweat". Biosensors 12, nr 10 (12.10.2022): 865. http://dx.doi.org/10.3390/bios12100865.

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Abnormal protein phosphorylation may relate to diseases such as Alzheimer’s, schizophrenia, and Parkinson’s. Therefore, the real-time detection of phosphoproteins in sweat was of great significance for the early knowledge, detection, and treatment of neurological diseases. In this work, anatase/rutile TiO2 was in situ grown on the MXene surface to constructing the intercalation structure MXene@anatase/rutile TiO2 ternary heterostructure as a sensing platform for detecting phosphoprotein in sweat. Here, the intercalation structure of MXene acted as electron and diffusion channels for phosphoproteins. The in situ grown anatase/rutile TiO2 with n-n-type heterostructure provided specific adsorption sites for the phosphoproteins. The determination of phosphoprotein covered concentrations in sweat, with linear range from 0.01 to 1 mg/mL, along with a low LOD of 1.52 μM. It is worth noting that, since the macromolecular phosphoprotein was adsorbed on the surface of the material, the electrochemical signal gradually decreased with the increase of phosphoprotein concentration. In addition, the active sites in the MXene@anatase/rutile TiO2 ternary heterojunction and synergistic effect of the heterojunction were verified by first-principle calculations to further realize the response to phosphoproteins. Additionally, the effective diffusion capacity and mobility of phosphoprotein molecules in the ternary heterojunction structure were studied by molecular dynamics simulation. Furthermore, the constructed sensing platform showed high selectivity, repeatability, reproducibility, and stability, and this newly developed sensor can detect for phosphoprotein in actual sweat samples. This satisfactory sensing strategy could be promoted to realize the noninvasive and continuous detection of sweat.

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Rodríguez-Vázquez, Raquel, Daniel Mouzo i Carlos Zapata. "Phosphoproteome Analysis Using Two-Dimensional Electrophoresis Coupled with Chemical Dephosphorylation". Foods 11, nr 19 (7.10.2022): 3119. http://dx.doi.org/10.3390/foods11193119.

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Protein phosphorylation is a reversible post-translational modification (PTM) with major regulatory roles in many cellular processes. However, the analysis of phosphoproteins remains the most challenging barrier in the prevailing proteome research. Recent technological advances in two-dimensional electrophoresis (2-DE) coupled to mass spectrometry (MS) have enabled the identification, characterization, and quantification of protein phosphorylation on a global scale. Most research on phosphoproteins with 2-DE has been conducted using phosphostains. Nevertheless, low-abundant and low-phosphorylated phosphoproteins are not necessarily detected using phosphostains and/or MS. In this study, we report a comparative analysis of 2-DE phosphoproteome profiles using Pro-Q Diamond phosphoprotein stain (Pro-Q DPS) and chemical dephosphorylation of proteins with HF-P from longissimus thoracis (LT) muscle samples of the Rubia Gallega cattle breed. We found statistically significant differences in the number of identified phosphoproteins between methods. More specifically, we found a three-fold increase in phosphoprotein detection with the HF-P method. Unlike Pro-Q DPS, phosphoprotein spots with low volume and phosphorylation rate were identified by HF-P technique. This is the first approach to assess meat phosphoproteome maps using HF-P at a global scale. The results open a new window for 2-DE gel-based phosphoproteome analysis.

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Rodriguez Galvan, Joaquin, Brianna Donner, Cat Hoang Veseley, Patrick Reardon, Heather M. Forsythe, Jesse Howe, Gretchen Fujimura i Elisar Barbar. "Human Parainfluenza Virus 3 Phosphoprotein Is a Tetramer and Shares Structural and Interaction Features with Ebola Phosphoprotein VP35". Biomolecules 11, nr 11 (29.10.2021): 1603. http://dx.doi.org/10.3390/biom11111603.

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The human parainfluenza virus 3 (HPIV3) poses a risk for pneumonia development in young children and immunocompromised patients. To investigate mechanisms of HPIV3 pathogenesis, we characterized the association state and host protein interactions of HPIV3 phosphoprotein (HPIV3 P), an indispensable viral polymerase cofactor. Sequence analysis and homology modeling predict that HPIV3 P possesses a long, disordered N-terminal tail (PTAIL) a coiled-coil multimerization domain (PMD), similar to the well-characterized paramyxovirus phosphoproteins from measles and Sendai viruses. Using a recombinantly expressed and purified construct of PMD and PTAIL, we show that HPIV3 P in solution is primarily an alpha-helical tetramer that is stable up to 60 °C. Pulldown and isothermal titration calorimetry experiments revealed that HPIV3 P binds the host hub protein LC8, and turbidity experiments demonstrated a new role for LC8 in increasing the solubility of HPIV3 P in the presence of crowding agents such as RNA. For comparison, we show that the multimerization domain of the Zaire Ebola virus phosphoprotein VP35 is also a tetramer and binds LC8 but with significantly higher affinity. Comparative analysis of the domain architecture of various virus phosphoproteins in the order Mononegavirales show multiple predicted and verified LC8 binding motifs, suggesting its prevalence and importance in regulating viral phosphoprotein structures. Our work provides evidence for LC8 binding to phosphoproteins with multiple association states, either tetrameric, as in the HPIV3 and Ebola phosphoproteins shown here, or dimeric as in rabies virus phosphoprotein. Taken together the data suggest that the association states of a virus-specific phosphoprotein and the complex formed by binding of the phosphoprotein to host LC8 are important regulators of viral function.

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Qiao, Yuting, Lijuan Qiao, Peize Zhao, Peng Zhang, Fanbin Wu, Jiahui Zhang, Li Gao, Bingxin Liu i Lei Zhang. "Phosphoprotein Detection in Sweat Realized by Intercalation Structure 2D@3D g-C3N4@Fe3O4 Wearable Sensitive Motif". Biosensors 12, nr 6 (24.05.2022): 361. http://dx.doi.org/10.3390/bios12060361.

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Abnormal protein phosphorylation in sweat metabolites is closely related to cancer, cardiovascular disease, and other diseases. The real-time monitoring of phosphoproteins in sweat is significant for early monitoring of disease biomarkers. Here, a high-efficiency electrochemical sensor for phosphoprotein in sweat was realized by 2D@3D g-C3N4@Fe3O4 with intercalation structure. Common phosphoprotein β-Casein was selected to demonstrate the platform’s functionalities. The detection limit of g-C3N4@Fe3O4 could be as low as 9.7 μM, and the detection range was from 0.01 mg/mL to 1 mg/mL. In addition, the sensing platform showed good selectivity, reproducibility, and stability. We also investigated the effects of interface structure on adsorption properties and electronic properties of the g-C3N4 and Fe3O4 heterostructure using DFT. More electrons from Fe3O4 were transferred to g-C3N4, which increased the electrons in the energy band of N atoms and promoted the formation of stable N-H bonds with H atoms in phosphoproteins. We demonstrated phosphoprotein sensor functionality by measuring the phosphoprotein in human sweat during exercising. This work realizes a sensing platform for noninvasive and continuous detection of sweat phosphoproteins in wearable devices.

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Li, Qing, Jiong Zhang, Yi Fang, Yan Dai, Ping Jia, Ziyan Shen, Sujuan Xu, Xiaoqiang Ding i Feng Zhou. "Phosphoproteome Profiling of uEVs Reveals p-AQP2 and p-GSK3β as Potential Markers for Diabetic Nephropathy". Molecules 28, nr 14 (24.07.2023): 5605. http://dx.doi.org/10.3390/molecules28145605.

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Diabetic nephropathy (DN) contributes to increased morbidity and mortality among patients with diabetes and presents a considerable global health challenge. However, reliable biomarkers of DN have not yet been established. Phosphorylated proteins are crucial for disease progression. However, their diagnostic potential remains unexplored. In this study, we used ultra-high-sensitivity quantitative phosphoproteomics to identify phosphoproteins in urinary extracellular vesicles (uEVs) as potential biomarkers of DN. We detected 233 phosphopeptides within the uEVs, with 47 phosphoproteins exhibiting significant alterations in patients with DN compared to those in patients with diabetes. From these phosphoproteins, we selected phosphorylated aquaporin-2 (p-AQP2[S256]) and phosphorylated glycogen synthase kinase-3β (p-GSK3β[Y216]) for validation, as they were significantly overrepresented in pathway analyses and previously implicated in DN pathogenesis. Both phosphoproteins were successfully confirmed through Phos-tag western blotting in uEVs and immunohistochemistry staining in kidney sections, suggesting that phosphoprotein alterations in uEVs reflect corresponding changes within the kidney and their potential as candidate biomarkers for DN. Our research proposes the utilization of phosphoproteins in uEVs as a liquid biopsy, presenting a highly feasible diagnostic tool for kidney disease.

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Skubitz, K. M., J. R. Mendiola i M. S. Collett. "CD15 monoclonal antibodies react with a phosphotyrosine-containing protein on the surface of human neutrophils." Journal of Immunology 141, nr 12 (15.12.1988): 4318–23. http://dx.doi.org/10.4049/jimmunol.141.12.4318.

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Abstract mAb are useful as probes in the study of the roles of cell-surface components in neutrophil function. Many mAb that bind to human neutrophils react with the oligosaccharide lacto-N-fucopentaose III (CD15 antibodies). These antibodies, as well as several other widely used mAb reactive with human neutrophils, were employed to detect phosphoproteins present on these cells. Immunoprecipitation and subsequent gel electrophoresis of proteins from neutrophils labeled with [gamma-32P]ATP revealed a 170 to 190-kDa phosphoprotein specifically reactive with CD15 antibodies. No phosphoproteins were immunoprecipitated by CD11 or CD18 mAb. Phosphoamino acid analysis of the 170- to 190-kDa protein showed that it contained predominantly phosphotyrosine and a low level of phosphoserine. Recently, it was shown that this phosphoprotein is one of the major substrates of ecto-protein kinase activity on human neutrophils. The roles for the 170- to 190-kDa phosphoprotein and the ecto-protein kinase in neutrophil function remain to be determined.

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Moradi, Atieh, Shuaijian Dai, Emily Oi Ying Wong, Guang Zhu, Fengchao Yu, Hon-Ming Lam, Zhiyong Wang i in. "Isotopically Dimethyl Labeling-Based Quantitative Proteomic Analysis of Phosphoproteomes of Soybean Cultivars". Biomolecules 11, nr 8 (16.08.2021): 1218. http://dx.doi.org/10.3390/biom11081218.

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Isotopically dimethyl labeling was applied in a quantitative post-translational modification (PTM) proteomic study of phosphoproteomic changes in the drought responses of two contrasting soybean cultivars. A total of 9457 phosphopeptides were identified subsequently, corresponding to 4571 phosphoprotein groups and 3889 leading phosphoproteins, which contained nine kinase families consisting of 279 kinases. These phosphoproteins contained a total of 8087 phosphosites, 6106 of which were newly identified and constituted 54% of the current soybean phosphosite repository. These phosphosites were converted into the highly conserved kinase docking sites by bioinformatics analysis, which predicted six kinase families that matched with those newly found nine kinase families. The overly post-translationally modified proteins (OPP) occupies 2.1% of these leading phosphoproteins. Most of these OPPs are photoreceptors, mRNA-, histone-, and phospholipid-binding proteins, as well as protein kinase/phosphatases. The subgroup population distribution of phosphoproteins over the number of phosphosites of phosphoproteins follows the exponential decay law, Y = 4.13e−0.098X − 0.04. Out of 218 significantly regulated unique phosphopeptide groups, 188 phosphoproteins were regulated by the drought-tolerant cultivar under the water loss condition. These significantly regulated phosphoproteins (SRP) are mainly enriched in the biological functions of water transport and deprivation, methionine metabolic processes, photosynthesis/light reaction, and response to cadmium ion, osmotic stress, and ABA response. Seventeen and 15 SRPs are protein kinases/phosphatases and transcription factors, respectively. Bioinformatics analysis again revealed that three members of the calcium dependent protein kinase family (CAMK family), GmSRK2I, GmCIPK25, and GmAKINβ1 kinases, constitute a phosphor-relay-mediated signal transduction network, regulating ion channel activities and many nuclear events in this drought-tolerant cultivar, which presumably contributes to the development of the soybean drought tolerance under water deprivation process.

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Pongprayoon, Wasinee, Atikorn Panya, Janthima Jaresitthikunchai, Narumon Phaonakrop i Sittiruk Roytrakul. "Phosphoprotein Profile of Rice (Oryza sativa L.) Seedlings under Osmotic Stress after Pretreatment with Chitosan". Plants 11, nr 20 (15.10.2022): 2729. http://dx.doi.org/10.3390/plants11202729.

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This study aims to identify novel chitosan (CTS)-responsive phosphoproteins in Leung Pratew 123 (LPT123) and Khao Dawk Mali 105 (KDML105) as drought-sensitive rice cultivars and differences in the CTS response. Rice seeds were soaked in CTS solution before germination, and 2- and 4-week-old rice seedlings sprayed with CTS before osmotic stress comprised the following four groups: (1) seedlings treated with distilled water; (2) seedlings treated with CTS; (3) seedlings pretreated with distilled water and subjected to osmotic stress; and (4) seedlings pretreated with CTS and subjected to osmotic stress. Phosphoproteins of leaf tissues were enriched using immobilized metal affinity chromatography (IMAC) before tryptic digestion and analysis via LC-MS. Phosphoprotein profiling analyses led to the identification of 4721 phosphoproteins representing 1052 and 1040 unique phosphoproteins in the LPT123 and KDML105 seedlings, respectively. In response to CTS pretreatment before osmotic stress, 22 differently expressed proteins were discovered, of which 10 and 12 were identified in the LPT123 and KDML105, respectively. These proteins are typically involved in signaling, transport, protein folding, protein degradation, and metabolism. This study provides fruitful data to understand the signal transduction mechanisms of rice seedlings pretreated with CTS before exposure to osmotic stress.

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Ganju, RK, RG Shpektor, DG Brenner i MA Shipp. "CD10/neutral endopeptidase 24.11 is phosphorylated by casein kinase II and coassociates with other phosphoproteins including the lyn src- related kinase". Blood 88, nr 11 (1.12.1996): 4159–65. http://dx.doi.org/10.1182/blood.v88.11.4159.4159.

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Abstract CD10/neutral endopeptidase 24.11 (NEP) regulates peptidemediated proliferation of lymphoid progenitors and certain epithelial cells and is itself regulated by cellular proliferation. To further characterize mechanisms by which cell-surface signaling might regulate CD10/NEP expression, we determined whether CD10/NEP was phosphorylated and whether the enzyme co-associated with additional cellular phosphoproteins. The CD10/NEP cytoplasmic tall contains two consensus recognition sequences for casein kinase II (CKII), a serine and threonine kinase that increases in activity following peptide signaling. In standard in vitro kinase assays, CKII phosphorylated full-length recombinant CD10/NEP but did not phosphorylate a truncated CD10/NEP protein that lacked the transmembrane region and cytoplasmic tail. To determine whether CD10/NEP might interact with additional cellular phosphoproteins, in vitro kinase assays were performed on CD10/NEP immune complexes from Nalm-6 cells. Three additional tyrosine phosphoproteins of approximately 40 kD, approximately 58 kD, and approximately 75 kD were identified in the CD10/NEP immunoprecipitates. The approximately 56-kD CD10/NEP-associated phosphoprotein was immunoprecipitated with an anti-lyn antibody confirming its identity as the lyn src-related kinase. Taken together, these data indicate that CD10/NEP is itself phosphorylated by CKII and that CD10/NEP co- associates with additional tyrosine phosphoproteins including lyn.

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Ganju, RK, RG Shpektor, DG Brenner i MA Shipp. "CD10/neutral endopeptidase 24.11 is phosphorylated by casein kinase II and coassociates with other phosphoproteins including the lyn src- related kinase". Blood 88, nr 11 (1.12.1996): 4159–65. http://dx.doi.org/10.1182/blood.v88.11.4159.bloodjournal88114159.

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CD10/neutral endopeptidase 24.11 (NEP) regulates peptidemediated proliferation of lymphoid progenitors and certain epithelial cells and is itself regulated by cellular proliferation. To further characterize mechanisms by which cell-surface signaling might regulate CD10/NEP expression, we determined whether CD10/NEP was phosphorylated and whether the enzyme co-associated with additional cellular phosphoproteins. The CD10/NEP cytoplasmic tall contains two consensus recognition sequences for casein kinase II (CKII), a serine and threonine kinase that increases in activity following peptide signaling. In standard in vitro kinase assays, CKII phosphorylated full-length recombinant CD10/NEP but did not phosphorylate a truncated CD10/NEP protein that lacked the transmembrane region and cytoplasmic tail. To determine whether CD10/NEP might interact with additional cellular phosphoproteins, in vitro kinase assays were performed on CD10/NEP immune complexes from Nalm-6 cells. Three additional tyrosine phosphoproteins of approximately 40 kD, approximately 58 kD, and approximately 75 kD were identified in the CD10/NEP immunoprecipitates. The approximately 56-kD CD10/NEP-associated phosphoprotein was immunoprecipitated with an anti-lyn antibody confirming its identity as the lyn src-related kinase. Taken together, these data indicate that CD10/NEP is itself phosphorylated by CKII and that CD10/NEP co- associates with additional tyrosine phosphoproteins including lyn.

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Cardone, Christophe, Claire-Marie Caseau, Benjamin Bardiaux, Aurélien Thureaux, Marie Galloux, Monika Bajorek, Jean-François Eléouët, Marc Litaudon, François Bontems i Christina Sizun. "A Structural and Dynamic Analysis of the Partially Disordered Polymerase-Binding Domain in RSV Phosphoprotein". Biomolecules 11, nr 8 (17.08.2021): 1225. http://dx.doi.org/10.3390/biom11081225.

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The phosphoprotein P of Mononegavirales (MNV) is an essential co-factor of the viral RNA polymerase L. Its prime function is to recruit L to the ribonucleocapsid composed of the viral genome encapsidated by the nucleoprotein N. MNV phosphoproteins often contain a high degree of disorder. In Pneumoviridae phosphoproteins, the only domain with well-defined structure is a small oligomerization domain (POD). We previously characterized the differential disorder in respiratory syncytial virus (RSV) phosphoprotein by NMR. We showed that outside of RSV POD, the intrinsically disordered N-and C-terminal regions displayed a structural and dynamic diversity ranging from random coil to high helical propensity. Here we provide additional insight into the dynamic behavior of PCα, a domain that is C-terminal to POD and constitutes the RSV L-binding region together with POD. By using small phosphoprotein fragments centered on or adjacent to POD, we obtained a structural picture of the POD–PCα region in solution, at the single residue level by NMR and at lower resolution by complementary biophysical methods. We probed POD–PCα inter-domain contacts and showed that small molecules were able to modify the dynamics of PCα. These structural properties are fundamental to the peculiar binding mode of RSV phosphoprotein to L, where each of the four protomers binds to L in a different way.

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Wajsman, R., J. R. F. Walters i M. M. Weiser. "Identification and isolation of the phosphorylated intermediate of the calcium pump in rat intestinal basolateral membranes". Biochemical Journal 256, nr 2 (1.12.1988): 593–98. http://dx.doi.org/10.1042/bj2560593.

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Transport of Ca2+ by the ATP-dependent Ca2+ pump has been demonstrated previously in rat intestinal basolateral-membrane vesicles. To identify the Ca2+-pump protein, duodenal basolateral membranes were phosphorylated with [gamma-32P]ATP in the presence of Ca2+ and La3+, under conditions conducive for maximal formation of the phosphorylated intermediate of the Ca2+ pump. Four major phosphoprotein bands were seen on autoradiograms of acidic SDS/polyacrylamide gels; the properties of a phosphoprotein (pp) at 130 kDa (pp130) were consistent with those expected for the plasma-membrane Ca2+ pump. This phosphoprotein was markedly enhanced by La3+, exhibited the characteristics of an acyl-phosphate bond, was preferentially phosphorylated from ATP and inhibited by micromolar concentrations of vanadate. Another phosphoprotein of 115 kDa possibly represented the endoplasmic reticulum Ca2+ pump or a fragment of pp130. Other phosphoproteins of 75 and 95 kDa were predominantly expressions of alkaline phosphatase. Formation of pp130 was highest in duodenal basolateral-membrane preparations when compared with those of jejunum and ileum or other subcellular fractions. A similar correlation between Ca2+-pump activity and pp130 formation was not found in membranes from villus-tip and crypt cells or in vitamin D-deficient animals. pp130 was isolated as a single phosphoprotein by calmodulin-affinity chromatography. We conclude that pp130 represents the phosphorylated intermediate of the rat intestinal basolateral-membrane Ca2+ pump, which can be separated from other phosphoproteins using its properties as a calmodulin-binding protein.

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Rothman, Deborah M., E. James Petersson, M. Eugenio Vázquez, Gabriel S. Brandt, Dennis A. Dougherty i Barbara Imperiali. "Caged Phosphoproteins". Journal of the American Chemical Society 127, nr 3 (styczeń 2005): 846–47. http://dx.doi.org/10.1021/ja043875c.

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B. Yaffe, Michael, i Lewis C. Cantley. "Grabbing phosphoproteins". Nature 402, nr 6757 (listopad 1999): 30–31. http://dx.doi.org/10.1038/46925.

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Greengard, Paul. "Neuronal phosphoproteins". Molecular Neurobiology 1, nr 1-2 (marzec 1987): 81–119. http://dx.doi.org/10.1007/bf02935265.

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Kiss, E., I. Edes, Y. Sato, W. Luo, S. B. Liggett i E. G. Kranias. "beta-Adrenergic regulation of cAMP and protein phosphorylation in phospholamban-knockout mouse hearts". American Journal of Physiology-Heart and Circulatory Physiology 272, nr 2 (1.02.1997): H785—H790. http://dx.doi.org/10.1152/ajpheart.1997.272.2.h785.

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The stimulatory effects of beta-adrenergic agonists reflect increases in intracellular adenosine 3',5'-cyclic monophosphate (cAMP) levels and phosphorylation of key regulatory proteins in the heart. One of these phosphoproteins is phospholamban (PLB) in sarcoplasmic reticulum, and ablation of PLB is associated with attenuation of the contractile responses to beta-adrenergic stimulation in the mouse heart. To determine whether this attenuation of beta-stimulation is due to altered phosphorylation characteristics of the other key cardiac phosphoproteins and/or to compensatory responses occurring in the absence of PLB, PLB-knockout and wild-type hearts were perfused and their protein phosphorylation patterns examined. The beta-adrenergic receptor density, adenylyl cyclase activity, tissue cAMP levels, and the basal phosphoprotein pattern were similar between PLB-knockout and wild-type hearts. Isoproterenol perfusion resulted in similar increases in the tissue cAMP levels and the degree of phosphorylation of troponin I, C protein, and the 21-kDa microsomal protein in wild-type and PLB-knockout hearts. These findings indicate that the attenuation of isoproterenol-mediated increases in contractility of the PLB-knockout hearts is not due to alterations in the beta-adrenergic signal transduction pathway or the degree of phosphorylation of the key cardiac regulatory phosphoproteins in myofibrils and sarcolemma.

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Ozon, Sylvie, Antoine Guichet, Olivier Gavet, Siegfried Roth i André Sobel. "Drosophila Stathmin: A Microtubule-destabilizing Factor Involved in Nervous System Formation". Molecular Biology of the Cell 13, nr 2 (luty 2002): 698–710. http://dx.doi.org/10.1091/mbc.01-07-0362.

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Stathmin is a ubiquitous regulatory phosphoprotein, the generic element of a family of neural phosphoproteins in vertebrates that possess the capacity to bind tubulin and interfere with microtubule dynamics. Although stathmin and the other proteins of the family have been associated with numerous cell regulations, their biological roles remain elusive, as in particular inactivation of the stathmin gene in the mouse resulted in no clear deleterious phenotype. We identified stathmin phosphoproteins inDrosophila, encoded by a unique gene sharing the intron/exon structure of the vertebrate stathmin andstathmin family genes. They interfere with microtubule assembly in vitro, and in vivo when expressed in HeLa cells. Drosophila stathmin expression is regulated during embryogenesis: it is high in the migrating germ cells and in the central and peripheral nervous systems, a pattern resembling that of mammalian stathmin. Furthermore, RNA interference inactivation ofDrosophila stathmin expression resulted in germ cell migration arrest at stage 14. It also induced important anomalies in nervous system development, such as loss of commissures and longitudinal connectives in the ventral cord, or abnormal chordotonal neuron organization. In conclusion, a single Drosophilagene encodes phosphoproteins homologous to the entire vertebrate stathmin family. We demonstrate for the first time their direct involvement in major biological processes such as development of the reproductive and nervous systems.

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Qin, Xiaoxiao, Panpan Li, Shaowei Lu, Yanchuan Sun, Lifeng Meng, Jinghong Hao i Shuangxi Fan. "Phosphoproteomic analysis of lettuce (Lactuca sativa L.) reveals starch and sucrose metabolism functions during bolting induced by high temperature". PLOS ONE 15, nr 12 (29.12.2020): e0244198. http://dx.doi.org/10.1371/journal.pone.0244198.

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High temperatures induce early bolting in lettuce (Lactuca sativa L.), which decreases both quality and production. However, knowledge of the molecular mechanism underlying high temperature promotes premature bolting is lacking. In this study, we compared lettuce during the bolting period induced by high temperatures (33/25 °C, day/night) to which raised under controlled temperatures (20/13 °C, day/night) using iTRAQ-based phosphoproteomic analysis. A total of 3,814 phosphorylation sites located on 1,766 phosphopeptides from 987 phosphoproteins were identified after high-temperature treatment,among which 217 phosphoproteins significantly changed their expression abundance (116 upregulated and 101 downregulated). Most phosphoproteins for which the abundance was altered were associated with the metabolic process, with the main molecular functions were catalytic activity and transporter activity. Regarding the functional pathway, starch and sucrose metabolism was the mainly enriched signaling pathways. Hence, high temperature influenced phosphoprotein activity, especially that associated with starch and sucrose metabolism. We suspected that the lettuce shorten its growth cycle and reduce vegetative growth owing to changes in the contents of starch and soluble sugar after high temperature stress, which then led to early bolting/flowering. These findings improve our understanding of the regulatory molecular mechanisms involved in lettuce bolting.

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Nicholson, Garth A., James G. McLeod i Leone Luey. "Skeletal muscle phosphoproteins: Muscle-specific basal and cAMP-dependent phosphoprotein profiles". Experimental Neurology 93, nr 1 (lipiec 1986): 138–44. http://dx.doi.org/10.1016/0014-4886(86)90153-6.

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Boskey, Adele L. "Phosphoproteins and Biomineralization". Phosphorus, Sulfur, and Silicon and the Related Elements 144, nr 1 (1.01.1999): 189–92. http://dx.doi.org/10.1080/10426509908546214.

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Wagner, Volker, Gunther Geßner, Ines Heiland, Marc Kaminski, Susan Hawat, Kai Scheffler i Maria Mittag. "Analysis of the Phosphoproteome of Chlamydomonas reinhardtii Provides New Insights into Various Cellular Pathways". Eukaryotic Cell 5, nr 3 (marzec 2006): 457–68. http://dx.doi.org/10.1128/ec.5.3.457-468.2006.

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ABSTRACT The unicellular flagellated green alga Chlamydomonas reinhardtii has emerged as a model organism for the study of a variety of cellular processes. Posttranslational control via protein phosphorylation plays a key role in signal transduction, regulation of gene expression, and control of metabolism. Thus, analysis of the phosphoproteome of C. reinhardtii can significantly enhance our understanding of various regulatory pathways. In this study, we have grown C. reinhardtii cultures in the presence of an inhibitor of Ser/Thr phosphatases to increase the phosphoprotein pool. Phosphopeptides from these cells were enriched by immobilized metal-ion affinity chromatography and analyzed by nano-liquid chromatography-electrospray ionization-mass spectrometry (MS) with MS-MS as well as neutral-loss-triggered MS-MS-MS spectra. In this way, we were able to identify 360 phosphopeptides from 328 different phosphoproteins of C. reinhardtii, thus providing new insights into a variety of cellular processes, including metabolic and signaling pathways. Comparative analysis of the phosphoproteome also yielded new functional information on proteins controlled by redox regulation (thioredoxin target proteins) and proteins of the chloroplast 70S ribosome, the centriole, and especially the flagella, for which 32 phosphoproteins were identified. The high yield of phosphoproteins of the latter correlates well with the presence of several flagellar kinases and indicates that phosphorylation/dephosphorylation represents one of the key regulatory mechanisms of eukaryotic cilia. Our data also provide new insights into certain cilium-related mammalian diseases.

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Quiroga, Ivana, Mariana Regente, Luciana Pagnussat, Ana Maldonado, Jesús Jorrín i Laura de la Canal. "Phosphorylated 11S globulins in sunflower seeds". Seed Science Research 23, nr 3 (12.06.2013): 199–204. http://dx.doi.org/10.1017/s0960258513000160.

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AbstractHelianthinins are storage proteins present in Helianthus annuus seeds, belonging to the 11S globulin family. Here we describe that a fraction of the helianthinins is phosphorylated. This conclusion is supported by different criteria, including identification by matrix-assisted laser desorption/ionization-time of flight (MALDI-TOF) mass spectrometry of major protein bands revealed with a specific dye for phosphoproteins, anti-phosphoserine antibody and binding to a phosphoprotein affinity matrix. Moreover, we show that the phosphorylation status of helianthinins changes following germination.

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Zavialova, M. G., V. G. Zgoda, O. N. Kharybin i E. N. Nikolayev. "In vitro protein phosphorylation as a template for SRM method development". Biomeditsinskaya Khimiya 60, nr 6 (2014): 668–76. http://dx.doi.org/10.18097/pbmc20146006668.

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Phosphorylation is one of the most common posttranslational modification (PTM) of proteins. Main challenge of phosphoprotein detection is their low abundance comparing to abundance of unmodified proteins. The method of selected reactions monitoring (SRM) allows to perform very sensitive and selective analysis of desired PTMs. Using myelin basic protein (MBP) as a model we have developed a method for phosphoprotein detection by SRM. The method is based on obtaining of phosphoproteins in a reconstituted kinase system and following usage these phosphorylated protein as a template for the development of the SRM method. The developed method was successfully applied for detection of phosphopeptides of myelin basic protein in the samples of human brain glioma.

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Mikkat, Stefan, Sabine Fulda i Martin Hagemann. "A 2D gel electrophoresis-based snapshot of the phosphoproteome in the cyanobacterium Synechocystis sp. strain PCC 6803". Microbiology 160, nr 2 (1.02.2014): 296–306. http://dx.doi.org/10.1099/mic.0.074443-0.

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Cyanobacteria are photoautotrophic prokaryotes that occur in highly variable environments. Protein phosphorylation is one of the most widespread means to adjust cell metabolism and gene expression to the demands of changing growth conditions. Using a 2D gel electrophoresis-based approach and a phosphoprotein-specific dye, we investigated the protein phosphorylation pattern in cells of the model cyanobacterium Synechocystis sp. strain PCC 6803. The comparison of gels stained for total and phosphorylated proteins revealed that approximately 5 % of the protein spots seemed to be phosphoproteins, from which 32 were identified using MALDI-TOF MS. For eight of them the phosphorylated amino acid residues were mapped by subsequent mass spectrometric investigations of isolated phosphopeptides. Among the phosphoproteins, we found regulatory proteins, mostly putative anti-sigma factor antagonists, and proteins involved in translation. Moreover, a number of enzymes catalysing steps in glycolysis or the Calvin–Benson cycle were found to be phosphorylated, implying that protein phosphorylation might represent an important mechanism for the regulation of the primary carbon metabolism in cyanobacterial cells.

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Susa, Milorad, i Reinhard Marre. "Legionella pneumophila Invasion of MRC-5 Cells Induces Tyrosine Protein Phosphorylation". Infection and Immunity 67, nr 9 (1.09.1999): 4490–98. http://dx.doi.org/10.1128/iai.67.9.4490-4498.1999.

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ABSTRACT After uptake and intracellular multiplication of Legionella pneumophila in MRC-5 lung fibroblasts, important cytoskeletal filament structures, like actin, tubulin, or vimentin, and a cell membrane-associated fibronectin were rearranged during early infection, resulting in a loss of cell adhesion and collapse of the cytoskeleton. Dysregulation of the cellular phosphorylation and dephosphorylation cascade may contribute to the observed changes and may support intracellular survival and multiplication of L. pneumophila. We therefore studied expression of phosphoproteins during intracellular growth of L. pneumophila. By using an anti-tyrosine phosphoprotein antibody we showed that proteins phosphorylated on tyrosine residues accumulated progressively during late infection exclusively around or in phagosomes filled with bacteria. In contrast, expression of serine/threonine phosphoproteins did not change. To discern the origin of phosphorylated proteins, the host cells were treated with cycloheximide, an inhibitor of eukaryotic protein synthesis. The newly synthesized proteins were labeled metabolically with [35S]methionine-cysteine and immunoprecipitated with a phosphotyrosine-specific antibody. Sodium dodecyl sulfate gel electrophoresis gave evidence for synthesis of at least three protein clusters (160 to 200, 35 to 60, and 19 to 28 kDa) of Legionella origin that were phosphorylated on tyrosine residues 24 h after infection. Treatment of infected host cells with genistein, a tyrosine kinase inhibitor, revealed that tyrosine protein phosphorylation was not important for bacterial uptake but contributed to intracellular growth of L. pneumophila. Bacterial tyrosine phosphoproteins and the observed intracellular structural changes may be important to understanding the process involved in intracellular growth of L. pneumophila.

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Heyworth, PG, J. Ding, RW Erickson, DJ Lu, JT Curnutte i JA Badwey. "Protein phosphorylation in neutrophils from patients with p67-phox- deficient chronic granulomatous disease". Blood 87, nr 10 (15.05.1996): 4404–10. http://dx.doi.org/10.1182/blood.v87.10.4404.bloodjournal87104404.

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Neutrophils are known to contain a major 67-kD protein that undergoes enhanced phosphorylation and translocation to the membrane during cell stimulation. Recent studies have assumed that this 67-kD phosphoprotein is the 67-kD subunit of the phagocyte oxidase (p67-phox). We compare here the protein phosphorylation patterns in lysates of normal neutrophils and neutrophils from patients with chronic granulomatous disease (CGD) that are completely deficient in p67-phox. The phosphoproteins were labeled by incubation of the cells with radioactive inorganic phosphate (32Pi) or by the addition of [gamma- 32P]ATP to electropermeabilized neutrophils. With either method, stimulation of the normal or CGD cells always resulted in an enhanced incorporation of 32p into two proteins in the 67-kD area. The extent of phosphorylation of these two proteins was very similar in the normal and CGD cells when permeabilized neutrophils loaded with [gamma - 32P]ATP were compared. Moreover, no overall differences in the protein phosphorylation patterns were observed between the normal and CGD cells. Our data indicate that the major 67-kD phosphoproteins observed in stimulated neutrophils are clearly different from p67-phox.

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Meimoun, P., F. Ambard-Bretteville, C. Colas-des Francs-Small, B. Valot i J. Vidal. "Analysis of plant phosphoproteins". Analytical Biochemistry 371, nr 2 (grudzień 2007): 238–46. http://dx.doi.org/10.1016/j.ab.2007.08.022.

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Horne, William C., Heini Miettinen i Vincent T. Marchesi. "Erythrocyte membrane skeleton phosphoproteins: identification of two unrelated phosphoproteins in band 4.9". Biochimica et Biophysica Acta (BBA) - Biomembranes 944, nr 2 (październik 1988): 135–43. http://dx.doi.org/10.1016/0005-2736(88)90426-9.

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Tang, Qiuhan, Rui Zhao, Qi Lu i Guangyan Qing. "Magnetic Fe3O4@mTiO2-AIPA Microspheres for Separation of Phosphoproteins and Non-phosphoproteins". Journal of Wuhan University of Technology-Mater. Sci. Ed. 34, nr 3 (czerwiec 2019): 752–59. http://dx.doi.org/10.1007/s11595-019-2113-z.

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Waygood, E. Bruce, Roshan L. Mattoo, Ellen Erickson i Christian Vadeboncoeur. "Phosphoproteins and the phosphoenolpyruvate: sugar phosphotransferase system of Streptococcus salivarius. Detection of two different ATP-dependent phosphorylations of the phosphocarrier protein HPr". Canadian Journal of Microbiology 32, nr 4 (1.04.1986): 310–18. http://dx.doi.org/10.1139/m86-062.

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Phosphoproteins which arise from incubation of Streptococcus salivarius ATCC25975 crude extracts with [32P]phosphoenolpyruvate and [γ-32P] ATP, were separated and detected by sodium dodecyl sulphate – polyacrylamide gel electrophoresis and autoradiography. These procedures were carried out using the methodology that has been developed to allow for the detection of phosphoproteins containing 1-P-histidinyl and 3-P-histidinyl residues, and also to distinguish between these and phosphoproteins containing acid-stable phosphoamino acids such as phosphoserine, phosphothreonine, and phosphotyrosine. Extracts of cells which had been grown with various sugars as carbon sources were investigated to determine both constitutive and inducible phosphoproteins. No evidence was found for phosphoproteins specifically induced by a sugar, and in particular no evidence was found for any IIIsugar phosphocarrier protein of the phosphoenolpyruvate: sugar phosphotransferase system (PTS). Incubation with [γ-32P]ATP showed that histidine-containing phosphocarrier protein (HPr) of the PTS could be phosphorylated to give both acid-stable and acid-labile phosphoamino acid residues. The acid-labile ATP-dependent phosphorylation activity was activated by glucose-6-P and appeared to produce a 3-P-histidinyl residue in HPr.

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31

Nounurai, Prachumporn, Anis Afifah, Suthathip Kittisenachai i Sittiruk Roytrakul. "Phosphorylation of CAD1, PLDdelta, NDT1, RPM1 Proteins Induce Resistance in Tomatoes Infected by Ralstonia solanacearum". Plants 11, nr 6 (9.03.2022): 726. http://dx.doi.org/10.3390/plants11060726.

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Ralstonia solanacaerum is one of the most devastating bacteria causing bacterial wilt disease in more than 200 species of plants, especially those belonging to the family Solanaceae. To cope with this pathogen, plants have evolved different resistance mechanisms depending on signal transduction after perception. Phosphorylation is the central regulatory component of the signal transduction pathway. We investigated a comparative phosphoproteomics analysis of the stems of resistant and susceptible tomatoes at 15 min and 30 min after inoculation with Ralstonia solanacearum to determine the phosphorylated proteins involved in induced resistance. Phosphoprotein profiling analyses led to the identification of 969 phosphoproteins classified into 10 functional categories. Among these, six phosphoproteins were uniquely identified in resistant plants including cinnamyl alcohol dehydrogenase 1 (CAD1), mitogen-activated protein kinase kinase kinase 18 (MAPKKK18), phospholipase D delta (PLDDELTA), nicotinamide adenine dinucleotide transporter 1 (NDT1), B3 domain-containing transcription factor VRN1, and disease resistance protein RPM1 (RPM1). These proteins are typically involved in defense mechanisms across different plant species. qRT-PCR analyses were performed to evaluate the level of expression of these genes in resistant and susceptible tomatoes. This study provides useful data, leading to an understanding of the early defense mechanisms of tomatoes against R. solanacearum.

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Rattner, J. B., i D. P. Bazett-Jones. "Electron spectroscopic imaging of the centrosome in cells of the Indian muntjac". Journal of Cell Science 91, nr 1 (1.09.1988): 5–11. http://dx.doi.org/10.1242/jcs.91.1.5.

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Specific antibody labelling indicates that phosphoproteins are present at microtubule-organizing centres, including the centrosome. We have employed electron spectroscopic imaging techniques that permit high-resolution elemental analysis of thin sections of intact cells to investigate the precise distribution of phosphorus and therefore phosphoproteins at the centrosome of Indian muntjac cells. We report that these proteins are localized to both the pericentriolar matrix and the centriole. The matrix contains an abundance of phosphorus and is associated with microtubule elements. Within the mature centriole, major structures including the nine triplet blades and linking elements that connect adjacent blades are composed of phosphorylated proteins. In addition, phosphoproteins are abundant at the ends of the centriole, at the interface between the centriole lumen and the pericentriolar environment. From these observations we suggest that phosphoproteins may play both a structural and a functional role within the centrosome region.

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33

Mackey, A. J. "CRP: Cleavage of Radiolabeled Phosphoproteins". Nucleic Acids Research 31, nr 13 (1.07.2003): 3859–61. http://dx.doi.org/10.1093/nar/gkg513.

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Stukenberg, P. Todd, Kevin D. Lustig, Thomas J. McGarry, Randall W. King, Jian Kuang i Marc W. Kirschner. "Systematic identification of mitotic phosphoproteins". Current Biology 7, nr 5 (maj 1997): 338–48. http://dx.doi.org/10.1016/s0960-9822(06)00157-6.

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35

Saito, T., A. L. Arsenault, M. Yamauchi, Y. Kuboki i M. A. Crenshaw. "Mineral induction by immobilized phosphoproteins". Bone 21, nr 4 (październik 1997): 305–11. http://dx.doi.org/10.1016/s8756-3282(97)00149-x.

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36

Glimcher, M. Jacob, i Beatrice Lefteriou. "Soluble glycosylated phosphoproteins of cementum". Calcified Tissue International 45, nr 3 (maj 1989): 165–72. http://dx.doi.org/10.1007/bf02556060.

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LaJevic, Melissa Dawn, Sujatha Koduvayur, Lloyd H. Graf, Rhonna L. Cohen i Donald A. Chambers. "Phosphorylated mRNA binding proteins associated with NE/cAMP/PKA-mediated mRNA decay in S49 T lymphocytes (35.43)". Journal of Immunology 178, nr 1_Supplement (1.04.2007): S10. http://dx.doi.org/10.4049/jimmunol.178.supp.35.43.

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Abstract We have shown that norepinephrine (NE) mediates the β-adrenergic/cAMP/PKA-dependent mRNA destabilization of mRNAs in T lymphocytes. Our goal is to elucidate the mechanism(s) involved in NE mediated Thy-1 mRNA decay in S49 T lymphoma cells. NE signal transduction in S49 cells activates PKA which could lead to the phosphorylation of effector proteins involved in ARE mediated message decay. Previous results have identified AUF1, HuR, KSRP, TIAR, and Hsc70 as candidate effector proteins. This study analyzes phosphoproteins from S49 cells and the effect of NE treatment (150μM, 30 min) on phosphorylation. NE induced phosphorylation of PKA substrate in S49 cytoplasmic extract was identified at 47, 55, 60, and 105 kD via immunoblotting. Of the candidate proteins that correlate in size, only AUF1 and Hsc70 were detected in phosphoprotein isolated from S49 whole cell extract via affinity chromatography; however, their level of phosphorylation appears unchanged with NE treatment. To determine if other binding proteins may be PKA targets, a pull down assay using a biotinylated 170 nucleotide ARE rich Thy-1 probe and 32P metabolically labeled cytoplasmic protein (100μCi/ml, 30 min) isolated at least five phospho-binding protein, two of which, 60 kD and 105 kD, increased with NE treatment. These results characterize phosphoproteins that function in the NE-mediated decay of Thy-1 and other mRNAs. Supported by NIH

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38

Hu, Qin, Shaoqiang Hu, Zhenyang Zhang, Ximin Zhou, Shanshan Yang, Yuan Zhang i Xinguo Chen. "Fe3+-immobilized nanoparticle-modified capillary for capillary electrophoretic separation of phosphoproteins and non-phosphoproteins". ELECTROPHORESIS 32, nr 20 (27.09.2011): 2867–73. http://dx.doi.org/10.1002/elps.201100138.

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Jones, S. M. A., i S. J. Yeaman. "Phosphorylation of branched-chain 2-oxo acid dehydrogenase complex in isolated adipocytes. Effects of 2-oxo acids". Biochemical Journal 236, nr 1 (15.05.1986): 209–13. http://dx.doi.org/10.1042/bj2360209.

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Isolated adipocytes from rat epididymal fat-pads were incubated with [32P]Pi, and intracellular phosphoproteins were then analysed by SDS/polyacrylamide-gel electrophoresis and autoradiography. A phosphorylated polypeptide of apparent Mr 46,000 was identified as the alpha-subunit of branched-chain 2-oxo acid dehydrogenase complex by immunoprecipitation using antiserum raised against the homogeneous E1 component of branched-chain 2-oxo acid dehydrogenase complex. Immunoprecipitation of this phosphoprotein is blocked in a competitive manner by purified branched-chain 2-oxo acid dehydrogenase complex. Peptide mapping of the isolated phosphoprotein indicates that two sites on the polypeptide are phosphorylated in the intact cells. Addition of branched-chain 2-oxo acids to the incubation medium causes diminution in the extent of labelling of both phosphorylation sites on the alpha-subunit, an effect presumably mediated via their known inhibitory action on branched-chain 2-oxo acid dehydrogenase kinase. These observations provide direct evidence for phosphorylation of branched-chain 2-oxo acid dehydrogenase complex in intact cells.

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40

Garcia, Rodolfo C., Elena Banfi i Maria G. Pittis. "Infection of Macrophage-Like THP-1 Cells withMycobacterium avium Results in a Decrease in Their Ability to Phosphorylate Nucleolin". Infection and Immunity 68, nr 6 (1.06.2000): 3121–28. http://dx.doi.org/10.1128/iai.68.6.3121-3128.2000.

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ABSTRACT This study of the phosphorylation ability of macrophage-like cells upon infection with Mycobacterium avium was undertaken to establish potential targets of the interference with host response mechanisms. Cytosolic and membrane fractions from noninfected and infected cells were incubated with [γ-32P]ATP, in the presence of Mg2+ and the absence of Ca2+, and the patterns of phosphoproteins synthesized were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Lower levels of a 110-kDa phosphoprotein were observed in association with cytosolic fractions from mycobacterium-infected cells compared to noninfected cells or cells treated with lipopolysaccharide or having ingestedEscherichia coli or killed M. avium. The 110-kDa phosphoprotein was present in the soluble fraction (230,000 ×g supernatant) after the kinase incubation, from where it was partially purified and identified as phosphonucleolin by amino acid sequencing. The decrease in nucleolin phosphorylation observed was not related to changes in the cytosolic or membrane levels of this protein, and was detected also in the cytosolic fraction of32P-labeled intact cells.

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41

Ghosh, Rishila, Rakin Ahmed, Hafiz Ahmed i Bishnu P. Chatterjee. "Phosphorylated Proteins from Serum: A Promising Potential Diagnostic Biomarker of Cancer". International Journal of Molecular Sciences 23, nr 20 (15.10.2022): 12359. http://dx.doi.org/10.3390/ijms232012359.

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Cancer is a fatal disease worldwide. Each year ten million people are diagnosed around the world, and more than half of patients eventually die from it in many countries. A majority of cancer remains asymptomatic in the earlier stages, with specific symptoms appearing in the advanced stages when the chances of adequate treatment are low. Cancer screening is generally executed by different imaging techniques like ultrasonography (USG), mammography, CT-scan, and magnetic resonance imaging (MRI). Imaging techniques, however, fail to distinguish between cancerous and non-cancerous cells for early diagnosis. To confirm the imaging result, solid and liquid biopsies are done which have certain limitations such as invasive (in case of solid biopsy) or missed early diagnosis due to extremely low concentrations of circulating tumor DNA (in case of liquid biopsy). Therefore, it is essential to detect certain biomarkers by a noninvasive approach. One approach is a proteomic or glycoproteomic study which mostly identifies proteins and glycoproteins present in tissues and serum. Some of these studies are approved by the Food and Drug Administration (FDA). Another non-expensive and comparatively easier method to detect glycoprotein biomarkers is by ELISA, which uses lectins of diverse specificities. Several of the FDA approved proteins used as cancer biomarkers do not show optimal sensitivities for precise diagnosis of the diseases. In this regard, expression of phosphoproteins is associated with a more specific stage of a particular disease with high sensitivity and specificity. In this review, we discuss the expression of different serum phosphoproteins in various cancers. These phosphoproteins are detected either by phosphoprotein enrichment by immunoprecipitation using phosphospecific antibody and metal oxide affinity chromatography followed by LC-MS/MS or by 2D gel electrophoresis followed by MALDI-ToF/MS analysis. The updated knowledge on phosphorylated proteins in clinical samples from various cancer patients would help to develop these serum phophoproteins as potential diagnostic/prognostic biomarkers of cancer.

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Mikuni-Takagaki, Y., i M. J. Glimcher. "Post-translational processing of chicken bone phosphoproteins. Identification of the bone phosphoproteins of embryonic tibia". Biochemical Journal 268, nr 3 (15.06.1990): 585–91. http://dx.doi.org/10.1042/bj2680585.

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In order to understand the mechanism of the post-translational processing of bone phosphoproteins in embryonic bone, periosteal bone strips isolated from 12-day-embryonic-chick tibiae were cultured and the bone proteins labelled with Na2H32PO4. Of the total radiolabelled proteins recovered from the medium and bone extracts in the absence of SDS (‘medium’, ‘EDTA extract’ and ‘EDTA/guanidinium chloride extract’), nearly 80% of the radioactivity was found in the EDTA extract. The three major radiolabelled phosphoproteins in the EDTA extract of apparent Mr 68,000, 63,000 and 58,000 reacted with polyclonal as well as monoclonal antibodies raised against ‘32-kDa’ and ‘150-kDa’ bone phosphoproteins which were derived from 14-week-old chicken. Therefore these phosphorylated embryonic proteins are identified as chicken bone phosphoproteins. Judging from their common N-terminal sequences, differences in the patterns obtained by labelling them with several radioisotopes, and slightly different amino acid compositions, these components seem to have been derived from the same original protein by sequential proteolytic cleavage and other processing such as glycosylation and phosphorylation.

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Goshe, Michael B., Timothy D. Veenstra, Ellen A. Panisko, Thomas P. Conrads, Nicolas H. Angell i Richard D. Smith. "Phosphoprotein Isotope-Coded Affinity Tags: Application to the Enrichment and Identification of Low-Abundance Phosphoproteins". Analytical Chemistry 74, nr 3 (luty 2002): 607–16. http://dx.doi.org/10.1021/ac015528g.

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Suja, J. A., C. Antonio, A. Debec i J. S. Rufas. "Phosphorylated proteins are involved in sister-chromatid arm cohesion during meiosis I". Journal of Cell Science 112, nr 17 (1.09.1999): 2957–69. http://dx.doi.org/10.1242/jcs.112.17.2957.

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Sister-chromatid arm cohesion is lost during the metaphase I/anaphase I transition to allow homologue separation. To obtain needed information on this process we have analysed in grasshopper bivalents the sequential release of arm cohesion in relation to the behaviour of chromatid axes. Results show that sister axes are associated during early metaphase I but separate during late metaphase I leading to a concomitant change of chromosome structure that implies the loss of sister-kinetochore cohesion. Afterwards, homologues initiate their separation asynchronously depending on their size, and number and position of chiasmata. In all bivalents thin chromatin strands at the telomeres appeared as the last point of contact between sister chromatids. Additionally, we have analysed the participation of phosphoproteins recognised by the MPM-2 monoclonal antibody against mitotic phosphoproteins in arm cohesion in bivalents and two different kinds of univalents. Results show the absence of MPM-2 phosphoproteins at the interchromatid domain in mitotic chromosomes and meiotic univalents, but their presence in metaphase I bivalents. These phosphoproteins are lost at the onset of anaphase I. Taken together, these data have prompted us to propose a ‘working’ model for the release of arm cohesion during meiosis I. The model suggests that MPM-2 phosphoproteins may act as cohesive proteins associating sister axes. Their modification, once all bivalents are correctly aligned at the metaphase plate, would trigger a change of chromosome structure and the sequential release of sister-kinetochore, arm, and telomere cohesions.

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Utz, Paul J., Maria Hottelet, Walther J. van Venrooij i Paul Anderson. "Association of Phosphorylated Serine/Arginine (SR) Splicing Factors With The U1–Small Ribonucleoprotein (snRNP) Autoantigen Complex Accompanies Apoptotic Cell Death". Journal of Experimental Medicine 187, nr 4 (16.02.1998): 547–60. http://dx.doi.org/10.1084/jem.187.4.547.

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Proteins subject to proteolysis or phosphorylation during apoptosis are commonly precipitated by autoantibodies found in the serum of patients with systemic lupus erythematosus (SLE). We screened a panel of murine monoclonal and human monospecific sera reactive with known autoantigens for their ability to selectively precipitate phosphoproteins from apoptotic Jurkat T cell lysates. Sera known to recognize the U1–small nuclear ribonucleoprotein (snRNP) complex (confirmed by their ability to precipitate U1–snRNA) selectively precipitated a phosphoprotein complex (pp54, pp42, pp34, and pp23) from apoptotic lysates. Monoclonal antibodies reactive with U1–snRNP proteins precipitated the same phosphoprotein complex from apoptotic lysates. The phosphorylation and/or recruitment of these proteins to the U1–snRNP complex is induced by multiple apoptotic stimuli (e.g., Fas ligation, gamma irradiation, or UV irradiation), and is blocked by overexpression of bcl-2. The U1–snRNP-associated phosphoprotein complex is immunoprecipitated by monoclonal antibodies reactive with serine/arginine (SR) proteins that comprise a structurally related family of splicing factors. The association of phosphorylated SR proteins with the U1–snRNP complex in cells undergoing apoptosis suggests a mechanism for regulation of alternative splicing of apoptotic effector molecules.

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Arai, Miyuki M., Kenta Minami, Yukari Ogura, Nagisa Otsuka, Shohei Hama, Hiroshi Harayama, Mitsuhiro Sakase i Moriyuki Fukushima. "Variation among individual bulls in the distribution of acrosomal tyrosine-phosphorylated proteins in epididymal and ejaculated spermatozoa". Reproduction, Fertility and Development 29, nr 7 (2017): 1297. http://dx.doi.org/10.1071/rd15483.

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In Japanese black cattle, AI severely subfertile males have occasionally been found. In order to solve this problem, we previously asserted the need for exact examinations of acrosomal tyrosine-phosphorylated proteins and acrosome morphology in cryopreserved spermatozoa. In the present study, we further investigated acrosomal tyrosine-phosphorylated proteins in spermatozoa before cryopreservation and examined possible relationships between these phosphoproteins and acrosome stability. Ejaculated, epididymal and cryopreserved spermatozoa were subjected to examinations of general characteristics (motility, shape and acrosome morphology) and indirect immunofluorescence of acrosomal phosphoproteins. Unlike all general characteristic parameters, the distribution of acrosomal tyrosine-phosphorylated proteins in ejaculated and cauda epididymal spermatozoa varied considerably among bulls and was linked to the maintenance of morphologically normal acrosomes in cryopreserved spermatozoa or ejaculated spermatozoa after 270 min incubation. Moreover, the distribution of these phosphoproteins was arranged in the spermatozoa of the proximal epididymides. These findings indicate that acrosomal tyrosine-phosphorylated proteins are distributionally arranged during early process of sperm maturation, that their distribution of cauda epididymal and ejaculated spermatozoa are largely different among bulls, and that varied states of acrosomal phosphoproteins may result in individual differences in acrosome stability among bulls.

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Zhao, Xiaowei, Yunxia Qi, Tao Wu i Guanglong Cheng. "Phosphoproteomic Analysis of the Jejunum Tissue Response to Colostrum and Milk Feeding in Dairy Calves during the Passive Immunity Period". Animals 13, nr 1 (30.12.2022): 145. http://dx.doi.org/10.3390/ani13010145.

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Improvements in the feeding of calves are of increasing importance for the development of the dairy industry. While colostrum is essential for the health of newborn calves, knowledge of protein phosphorylation alterations in neonatal calves that are fed colostrum or mature milk is lacking. Here, mid-jejunum tissue samples were collected from calves that received colostrum or milk. Subsequently, the jejunum phosphoproteome was analyzed using a phosphopeptide enrichment method, i.e., titanium immobilized metal ion affinity chromatography, coupled with liquid chromatography-tandem mass spectrometry. A total of 2093 phosphopeptides carrying unique 1851 phosphorylation sites corresponding to 1180 phosphoproteins were identified. Of the 1180 phosphoproteins, 314 phosphorylation sites on 241 proteins were differentially expressed between the groups. Gene ontology analysis indicated that the phosphoproteins were strongly associated with developmental and macromolecule metabolic processes, signal transduction, and responses to stimuli and insulin. Pathway analysis showed that the spliceosome, Hippo, insulin, and neurotrophin signaling pathways were enriched. These results reveal the expression pattern and changes in the function of phosphoproteins in bovine jejunum tissues under different feeding conditions and provide further insights into the crucial role of colostrum feeding during the early stages of life.

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48

Zhang, Dawei, Zhenhua Zhou, Guifeng Sun, Shiying Chen, Minzhi Jiang, Zihan Yao, Anthony Chukwunonso Ogbuehi, Hao Wang i Lei Jin. "Simultaneous Adsorption of Intact Glycoproteins and Phosphoproteins Using Hydrophilic Titanium (IV) Ion-Immobilized Cotton Fiber Functionalized by Phytic Acid Assembly". Journal of Chemistry 2023 (6.06.2023): 1–10. http://dx.doi.org/10.1155/2023/9943919.

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Protein glycosylation and phosphorylation are two important post-translational modifications and play significant roles in various biological processes. However, both glycoproteins and phosphoproteins are in low abundance in complex samples, which hinders their characterization. In this work, we developed a novel method for the simultaneous adsorption of glycoproteins and phosphoproteins based on solid phase extraction. By virtue of the unique structure of hydrophilic titanium (IV) ion immobilized cotton fiber functionalized with phytic acid (denoted as Ti4+-PA-cotton), glycoproteins, and phosphoproteins could be efficiently enriched in one-step incubation and eluted in sequence. The newly prepared Ti4+-PA-cotton was well characterized, and the adsorption isotherms and kinetics were studied. The maximum adsorption capacities of Ti4+-PA-cotton for β-casein and HRP were 833.3 mg/g and 384.6 mg/g with the adsorption rate of 259.1 and 63.1 mg/g·min. Standard protein mixture of BSA, HRP, and β-casein was used to test the enrichment ability as a proof of concept. The SDS-PAGE results demonstrated that Ti4+-PA-cotton had an excellent enrichment performance and possessed an outstanding application potential in the analysis of glycoproteins and phosphoproteins.

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Zaffran, Y., J. C. Escallier, S. Ruta, C. Capo i J. L. Mege. "Zymosan-triggered association of tyrosine phosphoproteins and lyn kinase with cytoskeleton in human monocytes." Journal of Immunology 154, nr 7 (1.04.1995): 3488–97. http://dx.doi.org/10.4049/jimmunol.154.7.3488.

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Abstract Phagocytosis of pathogens and inert particles such as zymosan by macrophages, and related secretory functions require the combination of several intracellular signals and the reorganization of cytoskeleton. We recently reported that zymosan stimulated the tyrosine phosphorylations of several endogenous substrates in human monocytes. In this work, the relationship between zymosan-stimulated tyrosine phosphoproteins and detergent-insoluble material considered as cytoskeleton was investigated. Triton X-100-insoluble fraction contained two proteins of 53 and 56 kDa that were tyrosine phosphorylated after only 5 min of stimulation with zymosan and remained labeled for 30 min. Because 53- and 56-kDa phosphoproteins migrated, as did some components of the src tyrosine kinase family, namely p53-56lyn, we wondered if 53- and 56-kDa phosphoproteins were related to lyn kinase. First, the amount of immunoreactive p53-56lyn increased in Triton X-100-insoluble fraction as did zymosan-stimulated tyrosine phosphoproteins. This property of p53-56lyn was unique, as no other member of the src family was found in this fraction. Second, when the immunoblots were reprobed with anti-phosphotyrosine mAb, the m.w. of p53-56lyn and tyrosine-phosphorylated proteins were identical in apparent size. Third, p53-56lyn was probably activated after cell stimulation with zymosan, because the phosphorylation levels of a synthetic copolymer of glutamine-tyrosine were increased in Triton X-100-insoluble fraction. In addition, we studied the distribution of lyn kinase and tyrosine phosphoproteins in phagocytozing monocytes. By using immunofluorescence, we showed that lyn kinase was located preferentially in the periphagosomal region in a specific manner, as an src tyrosine kinase such as p59hck, which was not associated with cytoskeleton, was not concentrated around the vacuoles. Moreover, periphagosomal phosphoproteins were also detected and found to be colocalized with polymerized actin. Because zymosan interacts with human monocytes via beta 2 integrins, which are known to be cytoskeleton-associated, we suggest that p53-56lyn provides the molecular link between zymosan receptors and cytoskeleton, and directs the cytoskeletal reorganization in the periphagosomal area.

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Baudouin, Emmanuel, Juliette Puyaubert, Patrice Meimoun, Mélisande Blein-Nicolas, Marlène Davanture, Michel Zivy i Christophe Bailly. "Dynamics of Protein Phosphorylation during Arabidopsis Seed Germination". International Journal of Molecular Sciences 23, nr 13 (24.06.2022): 7059. http://dx.doi.org/10.3390/ijms23137059.

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Seed germination is critical for early plantlet development and is tightly controlled by environmental factors. Nevertheless, the signaling networks underlying germination control remain elusive. In this study, the remodeling of Arabidopsis seed phosphoproteome during imbibition was investigated using stable isotope dimethyl labeling and nanoLC-MS/MS analysis. Freshly harvested seeds were imbibed under dark or constant light to restrict or promote germination, respectively. For each light regime, phosphoproteins were extracted and identified from dry and imbibed (6 h, 16 h, and 24 h) seeds. A large repertoire of 10,244 phosphopeptides from 2546 phosphoproteins, including 110 protein kinases and key regulators of seed germination such as Delay Of Germination 1 (DOG1), was established. Most phosphoproteins were only identified in dry seeds. Early imbibition led to a similar massive downregulation in dormant and non-dormant seeds. After 24 h, 411 phosphoproteins were specifically identified in non-dormant seeds. Gene ontology analyses revealed their involvement in RNA and protein metabolism, transport, and signaling. In addition, 489 phosphopeptides were quantified, and 234 exhibited up or downregulation during imbibition. Interaction networks and motif analyses revealed their association with potential signaling modules involved in germination control. Our study provides evidence of a major role of phosphosignaling in the regulation of Arabidopsis seed germination.

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