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Relevant bibliographies by topics / Phosphorylation

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Academic literature on the topic 'Phosphorylation'

Author: Grafiati

Published: 4 June 2021

Last updated: 16 November 2024

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Journal articles on the topic "Phosphorylation"

1

Hizli, Asli A., Yong Chi, Jherek Swanger, John H. Carter, Yi Liao, Markus Welcker, Alexey G. Ryazanov, and Bruce E. Clurman. "Phosphorylation of Eukaryotic Elongation Factor 2 (eEF2) by Cyclin A–Cyclin-Dependent Kinase 2 Regulates Its Inhibition by eEF2 Kinase." Molecular and Cellular Biology 33, no. 3 (November 26, 2012): 596–604. http://dx.doi.org/10.1128/mcb.01270-12.

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ABSTRACTProtein synthesis is highly regulated via both initiation and elongation. One mechanism that inhibits elongation is phosphorylation of eukaryotic elongation factor 2 (eEF2) on threonine 56 (T56) by eEF2 kinase (eEF2K). T56 phosphorylation inactivates eEF2 and is the only known normal eEF2 functional modification. In contrast, eEF2K undergoes extensive regulatory phosphorylations that allow diverse pathways to impact elongation. We describe a new mode of eEF2 regulation and show that its phosphorylation by cyclin A–cyclin-dependent kinase 2 (CDK2) on a novel site, serine 595 (S595), directly regulates T56 phosphorylation by eEF2K. S595 phosphorylation varies during the cell cycle and is required for efficient T56 phosphorylationin vivo. Importantly, S595 phosphorylation by cyclin A-CDK2 directly stimulates eEF2 T56 phosphorylation by eEF2Kin vitro, and we suggest that S595 phosphorylation facilitates T56 phosphorylation by recruiting eEF2K to eEF2. S595 phosphorylation is thus the first known eEF2 modification that regulates its inhibition by eEF2K and provides a novel mechanism linking the cell cycle machinery to translational control. Because all known eEF2 regulation is exerted via eEF2K, S595 phosphorylation may globally couple the cell cycle machinery to regulatory pathways that impact eEF2K activity.

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Coulonval, Katia, Hugues Kooken, and Pierre P. Roger. "Coupling of T161 and T14 phosphorylations protects cyclin B–CDK1 from premature activation." Molecular Biology of the Cell 22, no. 21 (November 2011): 3971–85. http://dx.doi.org/10.1091/mbc.e11-02-0136.

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Mitosis is triggered by the abrupt dephosphorylation of inhibitory Y15 and T14 residues of cyclin B1–bound cyclin-dependent kinase (CDK)1 that is also phosphorylated at T161 in its activation loop. The sequence of events leading to the accumulation of fully phosphorylated cyclin B1–CDK1 complexes remains unclear. Two-dimensional gel electrophoresis allowed us to determine whether T14, Y15, and T161 phosphorylations occur on same CDK1 molecules and to characterize the physiological occurrence of their seven phosphorylation combinations. Intriguingly, in cyclin B1–CDK1, the activating T161 phosphorylation never occurred without the T14 phosphorylation. This strict association could not be uncoupled by a substantial reduction of T14 phosphorylation in response to Myt1 knockdown, suggesting some causal relationship. However, T14 phosphorylation was not directly required for T161 phosphorylation, because Myt1 knockdown did uncouple these phosphorylations when leptomycin B prevented cyclin B1–CDK1 complexes from accumulating in cytoplasm. The coupling mechanism therefore depended on unperturbed cyclin B1–CDK1 traffic. The unexpected observation that the activating phosphorylation of cyclin B1–CDK1 was tightly coupled to its T14 phosphorylation, but not Y15 phosphorylation, suggests a mechanism that prevents premature activation by constitutively active CDK-activating kinase. This explained the opposite effects of reduced expression of Myt1 and Wee1, with only the latter inducing catastrophic mitoses.

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ADAMS, Ryan A., Xinran LIU, David S. WILLIAMS, and Alexandra C. NEWTON. "Differential spatial and temporal phosphorylation of the visual receptor, rhodopsin, at two primary phosphorylation sites in mice exposed to light." Biochemical Journal 374, no. 2 (September 1, 2003): 537–43. http://dx.doi.org/10.1042/bj20030408.

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Phosphorylation of rhodopsin critically controls the visual transduction cascade by uncoupling it from the G-protein transducin. The kinase primarily responsible for this phosphorylation is rhodopsin kinase, a substrate-regulated kinase that phosphorylates light-activated rhodopsin. Protein kinase C has been implicated in controlling the phosphorylation of both light-activated and dark-adapted rhodopsin. Two of the major rhodopsin phosphorylation sites in vivo, Ser334 and Ser338, are effective protein kinase C phosphorylation sites in vitro, while the latter is preferentially phosphorylated by rhodopsin kinase in vitro. Using phosphospecific antibodies against each of these two sites, we show that both sites are under differential spatial and temporal regulation. Exposure of mice to light results in rapid phosphorylation of Ser338 that is evenly distributed along the rod outer segment. Phosphorylation of Ser334 is considerably slower, begins at the base of the rod outer segment, and spreads to the top of the photoreceptor over time. In addition, we show that phosphorylation of both sites is abolished in rhodopsin kinase−/− mice, revealing an absolute requirement for rhodopsin kinase to phosphorylate rhodopsin. This requirement may reflect the need for priming phosphorylations at rhodopsin kinase sites allowing for subsequent phosphorylation by protein kinase C at Ser334. In this regard, treatment of mouse retinas with phorbol esters results in a 4-fold increase in phosphorylation on Ser334, with no significant effect on the phosphorylation of Ser338. Our results are consistent with light triggering rapid priming phosphorylations of rhodopsin by rhodopsin kinase, followed by a slower phosphorylation on Ser334, which is regulated by protein kinase C.

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Vanoosthuyse, Vincent, and Kevin G. Hardwick. "The Complexity of Bub1 Regulation: Phosphorylation, Phosphorylation, Phosphorylation." Cell Cycle 2, no. 2 (March 7, 2003): 118–19. http://dx.doi.org/10.4161/cc.2.2.343.

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Pant, Harish C., and Veeranna. "Neurofilament phosphorylation." Biochemistry and Cell Biology 73, no. 9-10 (September 1, 1995): 575–92. http://dx.doi.org/10.1139/o95-063.

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Neurofilament proteins (NFPs) are highly phosphorylated molecules in the axonal compartment of the adult nervous system. The phosphorylation of NFP is considered an important determinant of filament caliber, plasticity, and stability. This process reflects the function of NFs during the lifetime of a neuron from differentiation in the embryo through long-term activity in the adult until aging and environmental insult leads to pathology and ultimately death. NF function is modulated by phosphorylation–dephosphorylation in each of these diverse neuronal states. In this review, we have summarized some of these properties of NFP in adult nervous tissue, mostly from work in our own laboratory. Identification of sites phosphorylated in vivo in high molecular weight NFP (NF-H) and properties of NF-associated and neural-specific kinases phosphorylating specific sites in NFP are described. A model to explain the role of NF phosphorylation in determining filament caliber, plasticity, and stability is proposed.Key words: neurofilament proteins, phosphorylation, kinases, phosphatases, regulators, inhibitors, multimesic complex, domains.

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Bhattacharyya, Sumit, Alip Borthakur, Arivarasu N. Anbazhagan, Shivani Katyal, Pradeep K. Dudeja, and Joanne K. Tobacman. "Specific effects of BCL10 Serine mutations on phosphorylations in canonical and noncanonical pathways of NF-κB activation following carrageenan." American Journal of Physiology-Gastrointestinal and Liver Physiology 301, no. 3 (September 2011): G475—G486. http://dx.doi.org/10.1152/ajpgi.00071.2011.

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To determine the impact of B cell leukemia/lymphoma (BCL) 10 on the phosphorylation of crucial mediators in NF-κB-mediated inflammatory pathways, human colonic epithelial cells were exposed to carrageenan (CGN), a sulfated polysaccharide commonly used as a food additive and known to induce NF-κB nuclear translocation by both canonical and noncanonical pathways. Phosphorylations of intermediates in inflammatory cascades, including NF-κB-inducing kinase (NIK) at Thr559, transforming growth factor-β-activating kinase (TAK) 1 at Thr184, Thr187, and Ser192, and inhibitory factor κBα (IκBα) at Ser32, were examined following mutation of BCL10 at Ser138 and at Ser218. Specific phosphoantibodies were used for detection by enzyme-linked immunosorbent assay, immunoblot, and confocal microscopy of differences in phosphorylation following transfection by mutated BCL10. Both mutations demonstrated dominant-negative effects, with inhibition of phospho(Ser32)-IκBα to less than control levels. Both of the BCL10 mutations reduced the CGN-induced increases in nuclear RelA and p50, but only the Ser138 mutation inhibited the CGN-induced increases in nuclear RelB and p52 and in NIK Thr559 phosphorylation. Hence, the phosphorylation of BCL10 Ser138, but not Ser218, emerged as a critical event in activation of the noncanonical pathway of NF-κB activation. Either BCL10 Ser138 or Ser218 mutation inhibited the phosphorylation of TAK1 at Thr184 and at Thr187, but not at Ser192. These findings indicate that BCL10 phosphorylations act upstream of phosphorylations of NIK, TAK1, and IκBα and differentially affect the canonical and noncanonical pathways of NF-κB activation.

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Carty, DJ, DL Freas, and AR Gear. "ADP causes subsecond changes in protein phosphorylation of platelets." Blood 70, no. 2 (August 1, 1987): 511–15. http://dx.doi.org/10.1182/blood.v70.2.511.511.

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Abstract We developed a general quenched-flow approach to study platelet function as early as 0.3 seconds after stimulation. Phosphorylation of 20- and 47-kiloDalton (kD) proteins was analyzed during the first 5 seconds of platelet response to ADP from 0.5 to 10.0 mumol/L and compared with the progress of aggregation. The onset time for aggregation and phosphorylation of both proteins was less than 1 second; 20-K phosphorylation was increased greater than 200% and 47-K phosphorylation was increased 50%. The ADP sensitivity of 20-K phosphorylation was greater than that of 47-K phosphorylation (P less than .025), and of that of aggregation (P less than .01), with Ka values of 0.7, 1.0, and 1.2 mumol/L of ADP, respectively. The cyclooxygenase inhibitor indomethacin had no effect on aggregation, but inhibited both phosphorylations. Its inhibition of 20-K phosphorylation was greater than that of 47-K phosphorylation. Platelet activation by ADP thus induced biochemical changes well before 1 second. The quenched- flow approach may help to reveal relationships between phospholipase activation, calcium fluxes, and protein phosphorylation during these early periods of platelet activation.

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Carty, DJ, DL Freas, and AR Gear. "ADP causes subsecond changes in protein phosphorylation of platelets." Blood 70, no. 2 (August 1, 1987): 511–15. http://dx.doi.org/10.1182/blood.v70.2.511.bloodjournal702511.

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We developed a general quenched-flow approach to study platelet function as early as 0.3 seconds after stimulation. Phosphorylation of 20- and 47-kiloDalton (kD) proteins was analyzed during the first 5 seconds of platelet response to ADP from 0.5 to 10.0 mumol/L and compared with the progress of aggregation. The onset time for aggregation and phosphorylation of both proteins was less than 1 second; 20-K phosphorylation was increased greater than 200% and 47-K phosphorylation was increased 50%. The ADP sensitivity of 20-K phosphorylation was greater than that of 47-K phosphorylation (P less than .025), and of that of aggregation (P less than .01), with Ka values of 0.7, 1.0, and 1.2 mumol/L of ADP, respectively. The cyclooxygenase inhibitor indomethacin had no effect on aggregation, but inhibited both phosphorylations. Its inhibition of 20-K phosphorylation was greater than that of 47-K phosphorylation. Platelet activation by ADP thus induced biochemical changes well before 1 second. The quenched- flow approach may help to reveal relationships between phospholipase activation, calcium fluxes, and protein phosphorylation during these early periods of platelet activation.

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Kabachnik, M. I., L. S. Zakharov, E. I. Goryunov, and I. Yu Kudryavtsev. "Catalytic phosphorylation of polyfluoroalkanols. 11. ?-Polyfluoroalkylbenzyldichlorophosphates as phosphorylating agents in the catalytic phosphorylation of primary polyfluoroalkanols." Bulletin of the Academy of Sciences of the USSR Division of Chemical Science 38, no. 7 (July 1989): 1522–26. http://dx.doi.org/10.1007/bf00978451.

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Langlais, Paul, Zhengping Yi, and Lawrence J. Mandarino. "The Identification of Raptor as a Substrate for p44/42 MAPK." Endocrinology 152, no. 4 (February 15, 2011): 1264–73. http://dx.doi.org/10.1210/en.2010-1271.

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Abstract The adaptor protein raptor is the functional identifier for mammalian target of rapamycin (mTOR) complex 1 (mTORC1), acting to target mTOR to specific substrates for phosphorylation and regulation. Using HPLC-electrospray ionization tandem mass spectrometry, we confirmed the phosphorylation of raptor at Ser696, Thr706, Ser721, Ser722, Ser855, Ser859, Ser863, Thr865, Ser877, Ser881, Ser883, and Ser884 and identified Tyr692, Ser699, Thr700, Ser704, Ser854, Ser857, Ser882, Ser886, Ser887, and Thr889 as new, previously unidentified raptor phosphorylation sites. Treatment of cells with insulin increased the phosphorylation of raptor at Ser696, Ser855, Ser863, and Thr865 and suppressed the phosphorylation of Ser722. Ser696 phosphorylation was insensitive to mTOR inhibition with rapamycin, whereas treatment of cells with the MAPK inhibitor PD98059 inhibited the insulin-stimulated phosphorylation of raptor at Ser696. In vitro incubation of raptor with p42 MAPK significantly increased raptor phosphorylation (P < 0.01), whereas phosphorylation of a Ser696Ala mutant was decreased (P < 0.05), suggesting MAPK is capable of directly phosphorylating raptor at Ser696. Mutation of Ser696 to alanine interfered with insulin-stimulated phosphorylation of the mTOR downstream substrate p70S6 kinase. Incubation of cells with the MAPK inhibitor PD98059 and the phosphatidylinositol 3-kinase inhibitor wortmannin decreased the insulin stimulated phosphorylation of raptor, suggesting that the MAPK and phosphatidylinositol 3-kinase pathways may merge at mTORC1.

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Dissertations / Theses on the topic "Phosphorylation"

1

Hirose, Masayuki. "Phosphorylation and recruitment of Syk by ITAM-based phosphorylation of tamalin." Kyoto University, 2004. http://hdl.handle.net/2433/145291.

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Napper, Scott. "Phosphorylation sites of HPr." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape7/PQDD_0020/NQ43518.pdf.

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Craig, Timothy James. "Phosphorylation of exocytotic proteins." Thesis, University of Liverpool, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.406719.

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Ackerley, Steven. "Neurofilament transport and phosphorylation." Thesis, King's College London (University of London), 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.289881.

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Cleverly, Karen Elizabeth. "Investigation of neurofilament phosphorylation." Thesis, King's College London (University of London), 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.267652.

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Chaubey, Mark. "Phosphorylation of endocytic proteins." Thesis, University of Cambridge, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.615671.

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Thurston, Barbara. "Protein Phosphorylation in Archaea." Diss., Virginia Tech, 1997. http://hdl.handle.net/10919/30617.

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Protein phosphorylation constitutes an important mechanism for cellular regulation in both Eucarya and Bacteria. All living organisms evolved from a common progenitor; this implies that protein phosphorylation as a means of regulation also exists in Archaea. Previously, in the sulfur-dependent archaeon Sulfolobus solfataricus a gene was cloned encoding a protein-serine/threonine phosphatase that was similar to eucaryal protein-serine/threonine phosphatases type 1, 2A, and 2B. To identify protein phosphatases in other archaeons, oligonucleotides encoding conserved regions of eucaryal protein-serine/threonine phosphatases were used in the polymerase chain reaction to amplify genomic DNA from the methanogenic archaeon Methanosarcina thermophila. From the PCR reaction a fragment of DNA was isolated that encoded a portion of a protein phosphatase. Using this DNA fragment as a probe, the entire phosphatase gene was isolated. The amino acid sequence of the phosphatase encoded by this gene displayed greater than 30% identity with eucaryal protein-serine/threonine phosphatase type 1. The gene encoding the Methanosarcina phosphatase was expressed in Escherichia coli. The expressed protein exhibited protein serine phosphatase activity that was sensitive to inhibitors of eucaryal phosphatases such as okadaic acid, microcystin, calyculin, and tautomycin. In order to identify potential endogenous substrates of archaeal protein-serine/threonine phosphatases and kinases, a study was initiated to characterize the most prominent phosphoproteins in S. solfataricus. Cell extracts were incubated with [g-32P] ATP, MgCl2, and MnCl2, and the proteins in the extracts were separated by SDS-PAGE. Autoradiography of the gels revealed four prominent phosphoproteins with apparent molecular masses of 35, 46, and 50 kDa. N-terminal sequence analysis and enzymatic assays of the 35 kDa phosphoprotein identified this phosphoprotein as the a-subunit of succinyl-CoA synthetase. N-terminal sequence analysis and enzymatic assays revealed that the 50 kDa phosphoprotein was a hexosephosphate mutase. Neither the 50 kDa nor the 35 kDa phosphoprotein appeared to be the target of protein kinases or phosphatases. Therefore, while protein-serine phosphatases exist in Archaea, the targets of these phosphatases have yet to be determined.
Ph. D.

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Martins, Filipa de Sá. "Abeta dependent tau phosphorylation." Master's thesis, Universidade de Aveiro, 2011. http://hdl.handle.net/10773/7647.

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Mestrado em Biomedicina Molecular
Alzheimer’s disease (AD) is a neurodegenerative disorder characterized by the presence of two histopathological hallmarks: the extracellular amyloid plaques (APs) composed of beta-amyloid protein (Abeta) and intracellular neurofibrillary tangles (NFTs), containing hyperphosphorylated tau protein. Therefore, Abeta and tau are important molecules associated with AD and evidence suggests that Abeta may initiate the hyperphosphorylation of tau, which by disrupting neuronal network leads to the process of neurodegeneration. In the present study, using rat primary cortical and hippocampal neuronal cultures, it was shown that exposure to aggregated Abeta1-42 for prolonged periods decreased tau phosphorylation at Ser202 and Thr205 residue, but in contrast increased at Ser262 residue. Tau hyperphosphorylation in AD may be related to alterations in signal transduction pathways involving tau phosphorylation, such as an imbalance in the regulation of protein kinases (PKs) and protein phosphatases (PPs). Thus it is also important to determine which specific PKs and PPs are involved in this process. We observed the involvement of PP1 in the dephosphorylation of tau at Ser202 and Thr205, and the involvement of PP1 and PP2A at the Ser262 residue. An important aspect of tau metabolism are its binding proteins, and to date many such proteins have already been described both in vitro and in vivo. The interactome of tau is shaped by its phosphorylation and so is crucial to map the crosstalk between normal and pathologically hyperphosphorylated tau. By co-immunoprecipitation we intend to identify proteins that interact with tau and more specifically with phosphorylated tau (p-Tau). Furthermore the effect of Abeta on this interactome should be forthcoming, which is relevant for AD tau pathology.
A doença de Alzheimer (DA) é uma doença neurodegenerativa caracterizada pela presença de duas características histopatológicas: as placas senis na matriz extracelular compostas por Beta-amilóide (Abeta) e as tranças neurofibrilhares intracelulares contendo proteína tau hiperfosforilada. Assim, o Abeta e a proteína tau são importantes moléculas associadas à DA e evidências sugerem que o Abeta possa mediar a hiperfosforilação da tau levando á disrupção da rede neuronal e consequentemente ao processo de neurodegeneração. No presente estudo, em culturas primárias neuronais de córtex e hipocampo de rato, verificou-se que a exposição a Abeta1-42 agregado por longos períodos diminui a fosforilação da tau nos resíduos Ser202 e Thr205 e, em contraste, aumenta a fosforilação no resíduo Ser262. Pensa-se que a hiperfosforilação da tau na DA pode estar relacionada com alterações nas vias de sinalização celular envolvidas no processo de fosforilação da tau, tais como alterações na regulação das cinases e das fosfatases. Deste modo, é também de extrema importância determinar as cinases e fosfatases envolvidas neste processo. Por tratamento de neurónios corticais com diferentes concentrações de ácido ocadéico (AO), um inibidor das fosfatases, verificamos o envolvimento da PP1 na desfosforilação da tau nos resíduos Ser202 e Thr205, bem como o envolvimento da PP1 e PP2A na desfosforilação do resíduo Ser262. Um outro aspecto importante do metabolismo da tau são as proteínas de ligação, e actualmente já foram descritas várias proteínas que interagem com a tau in vitro e in vivo. O interactoma da tau é regulado pela sua fosforilação e portanto é crucial estabelecer uma relação entre a tau normal e a tau patológica hiperfosforilada no que diz respeito às proteínas de ligação. Por co-imunoprecipitação de neurónios corticais pretendemos identificar proteínas de ligação à tau e especificamente à tau fosforilada, e ainda avaliar o efeito do Abeta neste interactoma. O interactoma da tau dependente da fosforilação e do Abeta é de particular relevância para a compreensão da DA.

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Rardin, Matthew James. "Reversible phosphorylation in mitochondria." Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 2008. http://wwwlib.umi.com/cr/ucsd/fullcit?p3331484.

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Thesis (Ph. D.)--University of California, San Diego, 2008.
Title from first page of PDF file (viewed Dec. 16, 2008). Available via ProQuest Digital Dissertations. Vita. Includes bibliographical references.

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Wang, Huachun. "Protein phosphorylation regulation in Arabidopsis." Diss., Columbia, Mo. : University of Missouri-Columbia, 2006. http://hdl.handle.net/10355/5896.

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Thesis (Ph. D.)--University of Missouri-Columbia, 2006.
The entire dissertation/thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file (which also appears in the research.pdf); a non-technical general description, or public abstract, appears in the public.pdf file. Title from title screen of research.pdf file (viewed on July 18, 2008) Vita. Includes bibliographical references.

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Books on the topic "Phosphorylation"

1

Eyers, Claire E., ed. Histidine Phosphorylation. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-4939-9884-5.

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2

1936-, Marks Friedrich, ed. Protein phosphorylation. Weinheim: VCH, 1996.

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1945-, Moudgil V. K., ed. Receptor phosphorylation. Boca Raton, Fla: CRC Press, 1989.

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M, Sefton Bartholomew, and Hunter Tony 1943-, eds. Protein phosphorylation. San Diego, Calif: Academic Press, 1998.

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Kadenbach, Bernhard, ed. Mitochondrial Oxidative Phosphorylation. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4614-3573-0.

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Doerig, Christian, Gerald Späth, and Martin Wiese, eds. Protein Phosphorylation in Parasites. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2013. http://dx.doi.org/10.1002/9783527675401.

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R, Shewry P., Halford N. G, and Hooley Richard, eds. Protein phosphorylation in plants. Oxford: Clarendon Press, 1996.

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1946-, Kemp Bruce E., ed. Peptides and protein phosphorylation. Boca Raton, Fla: CRC Press, 1990.

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Turner, Andrew Michael. Protein phosphorylation in "Rhodomicrobium vannielii". [s.l.]: typescript, 1987.

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Heilmeyer, L. M. G., ed. Signal Transduction and Protein Phosphorylation. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4757-0166-1.

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Book chapters on the topic "Phosphorylation"

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Frank, J. Howard, J. Howard Frank, Michael C. Thomas, Allan A. Yousten, F. William Howard, Robin M. Giblin-davis, John B. Heppner, et al. "Phosphorylation." In Encyclopedia of Entomology, 2850. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6359-6_2918.

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Jones, Simon. "Phosphorylation." In Biotechnology, 221–41. Weinheim, Germany: Wiley-VCH Verlag GmbH, 2008. http://dx.doi.org/10.1002/9783527620913.ch4.

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Veenstra, Timothy D. "Phosphorylation." In Proteomics for Biological Discovery, 265–89. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2019. http://dx.doi.org/10.1002/9781119081661.ch11.

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Baker, Julien S., Fergal Grace, Lon Kilgore, David J. Smith, Stephen R. Norris, Andrew W. Gardner, Robert Ringseis, et al. "Phosphorylation." In Encyclopedia of Exercise Medicine in Health and Disease, 703. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-540-29807-6_2867.

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Gooch, Jan W. "Phosphorylation." In Encyclopedic Dictionary of Polymers, 915. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_14487.

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Ellis, Jonathan J., and Boštjan Kobe. "Protein Phosphorylation." In Encyclopedia of Biophysics, 2037–40. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-16712-6_184.

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Nichols, R. Jeremy. "LRRK2 Phosphorylation." In Advances in Neurobiology, 51–70. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-49969-7_3.

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Baak, Marleen A., Bernard Gutin, Kim A. Krawczewski Carhuatanta, Stephen C. Woods, Heinz W. Harbach, Megan M. Wenner, Nina S. Stachenfeld, et al. "Oxidative Phosphorylation." In Encyclopedia of Exercise Medicine in Health and Disease, 679. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-540-29807-6_2816.

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Gooch, Jan W. "Oxidative Phosphorylation." In Encyclopedic Dictionary of Polymers, 912. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_14414.

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Avila, Jesús, and Félix Hernández. "Tau Phosphorylation." In Advances in Neurobiology, 73–82. New York, NY: Springer New York, 2010. http://dx.doi.org/10.1007/978-1-4419-6787-9_3.

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Conference papers on the topic "Phosphorylation"

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Gear, LR A., D. Freas, and J. D. Carty. "EARLY (< 5 SEC) PHOSPHORYLATIONS OF PLATELET PROTEINS FOLLOWING ACTIVATION BY ADP AND ADRENALIN, SEPARATELY AND IN COMBINATION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643640.

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Understanding the earliest events (< 1 sec) in signal transduction of platelets is important, since there is evicenee that “shape change,” aggregation and secretion can all begin within this period. We have employed a guenched-flow approach to study these early events and found that thrombin can induce rapid phosphorylation of myosin light-chain kinase (20K) and a 47K protein (Blood, 67, 1738, 1986). To investigate the role of rapid phosphorylations in platelet activation, we have studied the influence of adrenalin and ADP during early (0.3 to 5 sec) stimulation. Aggregation in washed human platelets was assessed by following the loss of single particles and phosphorylation by analysing 32P-labeled proteins after gel electrophoresis. 15 µM adrenalin (without ADP) did not initiate significant aggregation or phosphorylation of myosin light chain (MLC). Phosphorylation of the 47K protein was increased by 20% at 5 sec. 0.5 µM ADP did not induce significant aggregation, but increased phosphorylation of MLC by 130% and the 47 protein by 20%. The combination of 0.5 µM ADP and 15 uM adrenalin induced significant aggregation by 0,3 sec (7.6%), which increased to 25.6% by 5 sec. Interestingly, MLC or 47K protein phosphorylation was not increased above control levels. However, the phosphorylation of four other proteins (77K, 102K, 140K and 185K), which previously had been very rapid (<1 sec) and reversible with 0.5 µM ADP alone, was now maintained, peaking at 3 sec. 10 µM ADP caused small sustained increases in phosphorylation of the same proteins. Adrenalin also caused rapid increases in the phosphorylation of 27K, 213 and 250K proteins. High levels of ADP (10 µM) only increased the 213 and 250K proteins; therefore the 27K protein appears adrenalin specific. Analysis of these early platelet phosphorylations will help understand how they are linked to initiation and maintenance of aggregation. Supported by NIH HL-27014.

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Daniel, J. L., and M. Rigmaiden. "Evidence for Ca2+-independent phosphorylation of human platelet myosin." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644527.

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Phosphorylation of platelet myosin is thought to be required for activation of the contractile events occurring during platelet activation. At present the only known mechanism for Onitiating myosin phosphorylation is through a Ca2+-calmodulin-dependent activation of myosin light chain kinase. However, our previous studies using the fluorescent Ca2+-indicator quin2 indicated that both platelet shape change and myosin phosphorylation could be induced in an EGTA-containing media in the absence of a measurable change in cytosolic free Ca2+ concentration (Hallam, Daniel, Kendrick-Jones & Rink. Biochem. J. 232 (1985) 373). In order to confirm this finding, we fyave investigated the regulation of myosin phosphorylation usin^+a preparation of electrically-permeabilized platelets and Ca2+ buffers to control the internal Ca2+ concentration. Fifty percent myosin phosphorylation was obtained at 700 nM Ca2+. When thrombin (5 U/ml) was added to this system, this curve shifted both to the left and upward; 50% myosin phosphorylation was obtained at 400 nM Ca2+.A synthetic inhibitor of protein kinase C, H7, had no effect on myosin phosphorylation in the absence of agonist but did inhibit the thrombin-induced shift to left suggesting that protein kinase C may modulate myosin phosphorylation. We also compared the effects of H7 agonist-induced myosin phosphorylation and shape change in control and an quin2 loaded platelets. Comparable inhibition of both phosphorylation and the rate of shape change was observed with both quin2 and H7. Addition of H7 to quin2-loaded platelets resulted in complete inhibition of both agonist-induced shape change and myosin phosphorylation. These results indicate that both protein kinase C and Ca2+-dependent reactions are involved in complete expression of myosin phosphorylation in human platelets.

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Ayati, Marzieh, Danica Wiredja, Daniela Schlatzer, Goutham Narla, Mark R. Chance, and Mehmet Koyuturk. "MoBaS on Phosphorylation Data." In BCB '16: ACM International Conference on Bioinformatics, Computational Biology, and Health Informatics. New York, NY, USA: ACM, 2016. http://dx.doi.org/10.1145/2975167.2995267.

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Khaybrakhmanova, Elvira A., Stanislav V. Kozyrev, Tatyana V. Tyumkina, and Irina Yu Ponedel’kina. "Phosphorylation of Hyaluronic Acid." In International Electronic Conference on Synthetic Organic Chemistry. Basel Switzerland: MDPI, 2022. http://dx.doi.org/10.3390/ecsoc-26-13535.

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Shvetsova, Anastasiia, Michele Fiore, Peter Strazewski, and Isabelle Daniel. "Phosphorylation of prebiotic precursors." In Goldschmidt2021. France: European Association of Geochemistry, 2021. http://dx.doi.org/10.7185/gold2021.6016.

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Enouf, J., R. Bredoux, A. Giraud, N. Bourdeau, and S. Levy-Toledano. "POSSIBLE RELATIONSHIP BETWEEN THE 23-kDa PHOSPHOPROTEIN AND THE IP3 -INDUCED Ca2+RELEASE IN HUMAN PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644516.

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The regulation of Ca2+ concentration in human platelets involves intracellular membranes i.e. dense tubular system (DTS). Agonist-induced platelet activation generates inositol 1,4,5 trisphosphate (IP3) which is responsible for Ca2+ mobilization from DTS. However, its mechanism of action is still unknown. cAMP has been shown to regulate Ca2+ transport by isolated membrane vesicles. This effect was correlated with the phosphorylation of a 23 kDa protein. We investigated whether this phosphorylation could play a role in the mechanism of IP3-induced Ca release.We isolated a membrane fraction enriched in intracellular membranes, which actively sequesters Ca2++. The Ca2+ uptake was mediated by a characterized (Ca2+ + Mg2+)-ATPase of a molecular weight 120 kDa. As well, the characterization of the 23-kDa protein phosphorylation by the catalytic subunit of the cAMP dependent protein kinase (C. Sub.) has been achieved. IP^-induced Ca release was tested on our membrane preparations. The transient effect was maximal at one minute and a dose-response curve was obtained.The cAMP dependent phosphorylation of the 23-kDa protein increased the Ca2+ liberation induced by IP by two fold whatever the IP3 concentration. The addition on the protein kinase inhibitor inhibited the IP3 -induced Ca2+ release.The effect of IP3 on the cAMP-mediated phosphorylation of the 23-kDa protein has been examinated.A dose dependent stimu-ulation of the 23-kDa protein phosphorylation in the presence of C. Sub. was initiated by IP3. The maximal effect was observed after 1-2 min and obtained with an IP3 concentration similar to that producing the maximal calcium release. The stimulation of the phosphorylation by IP3 was detected in the absence of Ca2+ and in the presence of phosphatase inhibitors.Therefore, we suggest a possible correlation between cAMP dependent phosphorylation of the 23-kDa protein and the IP3-induced Ca2+ release in human platelet membrane vesicles.

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Cheng, Qiong, Mitsunori Ogihara, and Vineet Gupta. "Inferring conflict-sensitive phosphorylation dynamics." In the 2nd ACM Conference. New York, New York, USA: ACM Press, 2011. http://dx.doi.org/10.1145/2147805.2147864.

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Krejčová, Romana, Květoslava Horská, Ivan Votruba, and Antonín Holý. "Phosphorylation of enantiomers of HPMPG." In XIth Symposium on Chemistry of Nucleic Acid Components. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 1999. http://dx.doi.org/10.1135/css199902286.

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Huzoor-Akbar, H., and Khursheed Anwer. "EVIDENCE THAT ABNORMAL PLATELET AGGREGATION IN SPONTANEOUSLY HYPERTENSIVE RATS IS LINKED WITH PHOSPHOINOSITIDES TURNOVER AND PHOSPHORYLATION OF 47,000 DALTON PROTEIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643810.

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We have shown earlier that abnormal platelet aggregation in spontaneously hypertensive rats (SHR) is not caused by prostaglandins (Thromb. Res. 41, 555-566, 1986). In this study platelets from SHR and normotensive (Wistar Kyoto, WKY) rats were used to examine the role of phosphoinositides (Pins) and protein phosphorylation in increased platelet activation in hypertension. Thrombin (0.05 U/ml) induced rapid hydrolysis of phosphatidylinositol-4,5-bis-phosphate (PIP2), phosphatidyl-inositol-4-phosphate (PIP), and phosphatidylinositol (PI) in (32p)-pO4 labeled platelets. However, significantly greater hydrolysis of PIP2 and PI was seen in SHR platelets than in WKY platelets (see Table). Thrombin also caused two- to three-fold increased accumulation of phosphatidic acid (PA) in SHR platelets than in WKY platelets (see Table).Thrombin caused phosphorylation of 18,000 Dalton (P18) and 47, Dalton (P47) proteins in SHR and WKY Platelets. Significantly increased phosphorylation of P47 was seen at 5, 15, 60 and 240 seconds of incubation with thrombin in SHR platelets (60%, 68%, 98% and 91%) than in WKY platelets (13%, 37%, 44% and 47%). The extent of P18 phosphorylation was same in both SHR and WKY platelets. Aspirin (500 uM) did not affect phosphorylation of P47 or P18 in SHR or WKY Platelets. These data lead us to suggest that increased turnover of Pins and increased phosphorylation of P47 are involved in abnormal platelet aggregation in SHR (Supported in part by the COHC grant #86-01-A and the Ohio University College of Osteopathic Medicine).

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Ismail, Hamid D., Ahoi Jones, Jung H. Kim, Robert H. Newman, and B. K. C. Dukka. "Phosphorylation sites prediction using Random Forest." In 2015 IEEE 5th International Conference on Computational Advances in Bio and Medical Sciences (ICCABS). IEEE, 2015. http://dx.doi.org/10.1109/iccabs.2015.7344726.

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Reports on the topic "Phosphorylation"

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JOHN C WALKER. SYMPOSIUM ON PLANT PROTEIN PHOSPHORYLATION. Office of Scientific and Technical Information (OSTI), November 2011. http://dx.doi.org/10.2172/1028190.

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Granot, David, Richard Amasino, and Avner Silber. Mutual effects of hexose phosphorylation enzymes and phosphorous on plant development. United States Department of Agriculture, January 2006. http://dx.doi.org/10.32747/2006.7587223.bard.

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Research objectives 1) Analyze the combined effects of hexose phosphorylation and P level in tomato and Arabidopsis plants 2) Analyze the combined effects of hexose phosphorylation and P level in pho1 and pho2 Arabidopsis mutants 3) Clone and analyze the PHO2 gene 4) Select Arabidopsis mutants resistant to high and low P 5) Analyze the Arabidopsis mutants and clone the corresponding genes 6) Survey wild tomato species for growth characteristics at various P levels Background to the topic Hexose phosphorylating enzymes, the first enzymes of sugar metabolism, regulate key processes in plants such as photosynthesis, growth, senescence and vascular transport. We have previously discovered that hexose phosphorylating enzymes might regulate these processes as a function of phosphorous (P) concentration, and might accelerate acquisition of P, one of the most limiting nutrients in the soil. These discoveries have opened new avenues to gain fundamental knowledge about the relationship between P, sugar phosphorylation and plant development. Since both hexose phosphorylating enzymes and P levels affect plant development, their interaction is of major importance for agriculture. Due to the acceleration of senescence caused by the combined effects of hexose phosphorylation and P concentration, traits affecting P uptake may have been lost in the course of cultivation in which fertilization with relatively high P (30 mg/L) are commonly used. We therefore intended to survey wild tomato species for high P-acquisition at low P soil levels. Genetic resources with high P-acquisition will serve not only to generate a segregating population to map the trait and clone the gene, but will also provide a means to follow the trait in classical breeding programs. This approach could potentially be applicable for other crops as well. Major conclusions, solutions, achievements Our results confirm the mutual effect of hexose phosphorylating enzymes and P level on plant development. Two major aspects of this mutual effect arose. One is related to P toxicity in which HXK seems to play a major role, and the second is related to the effect of HXK on P concentration in the plant. Using tomato plants we demonstrated that high HXK activity increased leaf P concentration, and induced P toxicity when leaf P concentration increases above a certain high level. These results further support our prediction that the desired trait of high-P acquisition might have been lost in the course of cultivation and might exist in wild species. Indeed, in a survey of wild species we identified tomato species that acquired P and performed better at low P (in the irrigation water) compared to the cultivated Lycopersicon esculentum species. The connection between hexose phosphorylation and P toxicity has also been shown with the P sensitive species VerticordiaplumosaL . in which P toxicity is manifested by accelerated senescence (Silber et al., 2003). In a previous work we uncovered the phenomenon of sugar induced cell death (SICD) in yeast cells. Subsequently we showed that SICD is dependent on the rate of hexose phosphorylation as determined by Arabidopsis thaliana hexokinase. In this study we have shown that hexokinase dependent SICD has many characteristics of programmed cell death (PCD) (Granot et al., 2003). High hexokinase activity accelerates senescence (a PCD process) of tomato plants, which is further enhanced by high P. Hence, hexokinase mediated PCD might be a general phenomena. Botrytis cinerea is a non-specific, necrotrophic pathogen that attacks many plant species, including tomato. Senescing leaves are particularly susceptible to B. cinerea infection and delaying leaf senescence might reduce this susceptibility. It has been suggested that B. cinerea’s mode of action may be based on induction of precocious senescence. Using tomato plants developed in the course of the preceding BARD grant (IS 2894-97) and characterized throughout this research (Swartzberg et al., 2006), we have shown that B. cinerea indeed induces senescence and is inhibited by autoregulated production of cytokinin (Swartzberg et al., submitted). To further determine how hexokinase mediates sugar effects we have analyzed tomato plants that express Arabidopsis HXK1 (AtHXK1) grown at different P levels in the irrigation water. We found that Arabidopsis hexokinase mediates sugar signalling in tomato plants independently of hexose phosphate (Kandel-Kfir et al., submitted). To study which hexokinase is involved in sugar sensing we searched and identified two additional HXK genes in tomato plants (Kandel-Kfir et al., 2006). Tomato plants have two different hexose phosphorylating enzymes; hexokinases (HXKs) that can phosphorylate either glucose or fructose, and fructokinases (FRKs) that specifically phosphorylate fructose. To complete the search for genes encoding hexose phosphorylating enzymes we identified a forth fructokinase gene (FRK) (German et al., 2004). The intracellular localization of the four tomato HXK and four FRK enzymes has been determined using GFP fusion analysis in tobacco protoplasts (Kandel-Kfir et al., 2006; Hilla-Weissler et al., 2006). One of the HXK isozymes and one of the FRK isozymes are located within plastids. The other three HXK isozymes are associated with the mitochondria while the other three FRK isozymes are dispersed in the cytosol. We concluded that HXK and FRK are spatially separated in plant cytoplasm and accordingly might play different metabolic and perhaps signalling roles. We have started to analyze the role of the various HXK and FRK genes in plant development. So far we found that LeFRK2 is required for xylem development (German et al., 2003). Irrigation with different P levels had no effect on the phenotype of LeFRK2 antisense plants. In the course of this research we developed a rapid method for the analysis of zygosity in transgenic plants (German et al., 2003).

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Davisson, Vincent J., Anthony Pedley, Qingshou Chen, Matthew Bartolowits, and Raymond Fatig. Targeting PCNA Phosphorylation in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, April 2012. http://dx.doi.org/10.21236/ada586048.

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Davisson, Vincent J., Anthony Pedley, Qingshou Chen, Matthew Bartolowits, and Raymond Fatig. Targeting PCNA Phosphorylation in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, April 2013. http://dx.doi.org/10.21236/ada586063.

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Davisson, Vincent J., Anthony Pedley, Qingshou Chen, and Matthew Bartolowits. Targeting PCNA Phosphorylation in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, April 2011. http://dx.doi.org/10.21236/ada554228.

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Karen S. Browning. Protein Synthesis Initiation Factors: Phosphorylation and Regulation. Office of Scientific and Technical Information (OSTI), June 2009. http://dx.doi.org/10.2172/956983.

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Dickman, Martin B., and Oded Yarden. Role of Phosphorylation in Fungal Spore Germination. United States Department of Agriculture, August 1993. http://dx.doi.org/10.32747/1993.7568761.bard.

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Spore germination is a common and fundamental event in fungal development and in many instances an essential phase of fungal infection and dissemination. Spore germination is also critical for hyperparasites to function as biocontrol agents as well as in fermentation proceses. Our common objective is to understand the mechanisms which regulated spore germination and identify factors involved in pathogenicity related prepenetration development. Our approach is to exploit the overall similarity among filamentous fungi using both a plant pathogen (Colletotricum trifolii) and a model system that is genetically sophisticated (Neurospora crassa). The simulataneous use of two organisms has the advantage of the available tools in Neurospora to rapidly advance the functional analysis of genes involved in spore germination and development of an economically important fungal phytopathogen. Towards this we have isolated a protein kinase gene from C. trifolii (TB3) that is maximally expressed during the first hour of conidial germination and prior to any visible gene tube formation. Based on sequence similarities with other organisms, this gene is likely to be involved in the proliferative response in the fungus. In addition, TB3 was able to functionally complement a N. crassa mutant (COT-1). Pharmacological studies indicated the importance of calmodulin in both germination and appressorium differentiation. Using an antisense vector from N. crassa, direct inhibition of calmodulin results in prevention of differentiation as well as pathogenicity. Both cAMP dependent protein kinase (PKA) and protein kinase C (PKC) like genes have been cloned from C. trifolii. Biochemical inhibition of PKA prevents germination; biochemical inhibitors of PKC prevents appressorium differentiation. In order to analyze reversible phosphorylation as a regulatory mechanism, some ser.thr dephosphorylative events have also been analyzed. Type 2A and Type 2B (calcineurin) phosphatases have been identified and structurally and functionally analyzed in N. crassa during this project. Both phosphatases are essential for hyphal growth and maintenance of proper hyphal architecture. In addition, a first novel-type (PPT/PP5-like) ser/thr phosphatase has been identified in a filamentous fungus. The highly collaborative project has improved our understanding of a fundamental process in fungi, and has identified targets which can be used to develop new approaches for control of fungal plant pathogens as well as improve the performance of beneficial fungi in the field and in industry. In addition, the feasibility of molecular technology transfer in comparative mycology has been demonstrated.

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Greengard, P. Role of Protein Phosphorylation in Regulation of Bioreactivity. Fort Belvoir, VA: Defense Technical Information Center, March 1985. http://dx.doi.org/10.21236/ada158875.

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Vasquez, Fancisca. Regulation of the Tumor Suppressor Protein PTEN by Phosphorylation. Fort Belvoir, VA: Defense Technical Information Center, July 2001. http://dx.doi.org/10.21236/ada398955.

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Vazquez, Francisca. Regulation of the Tumor Suppressor Protein PTEN by Phosphorylation. Fort Belvoir, VA: Defense Technical Information Center, July 2000. http://dx.doi.org/10.21236/ada392383.

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