Relevant bibliographies by topics / "CK2,Substrate,Identification"

Academic literature on the topic '"CK2,Substrate,Identification"'

Author: Grafiati
Published: 11 March 2023

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Journal articles on the topic ""CK2,Substrate,Identification""

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Calvert, Meredith E. K., Kristin M. Keck, Celeste Ptak, Jeffrey Shabanowitz, Donald F. Hunt, and Lucy F. Pemberton. "Phosphorylation by Casein Kinase 2 Regulates Nap1 Localization and Function." Molecular and Cellular Biology 28, no. 4 (December 17, 2007): 1313–25. http://dx.doi.org/10.1128/mcb.01035-07.

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ABSTRACT In Saccharomyces cerevisiae, the evolutionarily conserved nucleocytoplasmic shuttling protein Nap1 is a cofactor for the import of histones H2A and H2B, a chromatin assembly factor and a mitotic factor involved in regulation of bud formation. To understand the mechanism by which Nap1 function is regulated, Nap1-interacting factors were isolated and identified by mass spectrometry. We identified several kinases among these proteins, including casein kinase 2 (CK2), and a new bud neck-associated protein, Nba1. Consistent with our identification of the Nap1-interacting kinases, we showed that Nap1 is phosphorylated in vivo at 11 sites and that Nap1 is phosphorylated by CK2 at three substrate serines. Phosphorylation of these serines was not necessary for normal bud formation, but mutation of these serines to either alanine or aspartic acid resulted in cell cycle changes, including a prolonged S phase, suggesting that reversible phosphorylation by CK2 is important for cell cycle regulation. Nap1 can shuttle between the nucleus and cytoplasm, and we also showed that CK2 phosphorylation promotes the import of Nap1 into the nucleus. In conclusion, our data show that Nap1 phosphorylation by CK2 appears to regulate Nap1 localization and is required for normal progression through S phase.
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Bai, Xiyuan, Derek Silvius, Edward D. Chan, Denise Escalier, and Shaun Xin Xu. "Identification and characterization of a novel testis-specific gene CKT2 , which encodes a substrate for protein kinase CK2." Nucleic Acids Research 37, no. 8 (March 9, 2009): 2699–711. http://dx.doi.org/10.1093/nar/gkp094.

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Liu, Shan-shan, Hong-xia Zheng, Hua-dong Jiang, Jie He, Yang Yu, You-peng Qu, Lei Yue, Yao Zhang, and Yu Li. "Identification and characterization of a novel gene, c1orf109, encoding a CK2 substrate that is involved in cancer cell proliferation." Journal of Biomedical Science 19, no. 1 (2012): 49. http://dx.doi.org/10.1186/1423-0127-19-49.

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Holland, Zoë, Renaud Prudent, Jean-Baptiste Reiser, Claude Cochet, and Christian Doerig. "Functional Analysis of Protein Kinase CK2 of the Human Malaria Parasite Plasmodium falciparum." Eukaryotic Cell 8, no. 3 (December 29, 2008): 388–97. http://dx.doi.org/10.1128/ec.00334-08.

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ABSTRACT Protein kinase CK2 (casein kinase 2) is a eukaryotic serine/threonine protein kinase with multiple substrates and roles in diverse cellular processes, including differentiation, proliferation, and translation. The mammalian holoenzyme consists of two catalytic alpha or alpha′ subunits and two regulatory beta subunits. We report the identification and characterization of a Plasmodium falciparum CK2α orthologue, PfCK2α, and two PfCK2β orthologues, PfCK2β1 and PfCK2β2. Recombinant PfCK2α possesses protein kinase activity, exhibits similar substrate and cosubstrate preferences to those of CK2α subunits from other organisms, and interacts with both of the PfCK2β subunits in vitro. Gene disruption experiments show that the presence of PfCK2α is crucial to asexual blood stage parasites and thereby validate the enzyme as a possible drug target. PfCK2α is amenable to inhibitor screening, and we report differential susceptibility between the human and P. falciparum CK2α enzymes to a small molecule inhibitor. Taken together, our data identify PfCK2α as a potential target for antimalarial chemotherapeutic intervention.
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Gyenis, Laszlo, James S. Duncan, Jacob P. Turowec, Maria Bretner, and David W. Litchfield. "Unbiased Functional Proteomics Strategy for Protein Kinase Inhibitor Validation and Identification ofbona fideProtein Kinase Substrates: Application to Identification of EEF1D as a Substrate for CK2." Journal of Proteome Research 10, no. 11 (November 4, 2011): 4887–901. http://dx.doi.org/10.1021/pr2008994.

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Gyenis, Laszlo, Jacob P. Turowec, Maria Bretner, and David W. Litchfield. "Chemical proteomics and functional proteomics strategies for protein kinase inhibitor validation and protein kinase substrate identification: Applications to protein kinase CK2." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1834, no. 7 (July 2013): 1352–58. http://dx.doi.org/10.1016/j.bbapap.2013.02.006.

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Trujillo, Ramon, Francesc Miró, Maria Plana, Marta José, Mathieu Bollen, Willy Stalmans, and Emilio Itarte. "Substrates for Protein Kinase CK2 in Insulin Receptor Preparations from Rat Liver Membranes: Identification of a 210-kDa Protein Substrate as the Dimeric Form of Endoplasmin." Archives of Biochemistry and Biophysics 344, no. 1 (August 1997): 18–28. http://dx.doi.org/10.1006/abbi.1997.0155.

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Vetter, Daniel, Roland Kissmehl, Tilman Treptau, Karin Hauser, Josef Kellermann, and Helmut Plattner. "Molecular Identification of a Calcium-Inhibited Catalytic Subunit of Casein Kinase Type 2 from Paramecium tetraurelia." Eukaryotic Cell 2, no. 6 (December 2003): 1220–33. http://dx.doi.org/10.1128/ec.2.6.1220-1233.2003.

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ABSTRACT We have previously described the occurrence in Paramecium of a casein kinase (CK) activity (EC 2.7.1.37) with some unusual properties, including inhibition by Ca2+ (R. Kissmehl, T. Treptau, K. Hauser, and H. Plattner, FEBS Lett. 402:227-235, 1995). We now have cloned four genes, PtCK2α1 to PtCK2α4, all of which encode the catalytic α subunit of type 2 CK (CK2) with calculated molecular masses ranging from 38.9 to 39.4 kDa and pI values ranging from 8.8 to 9.0. They can be classified into two groups, which differ from each other by 28% on the nucleotide level and by 18% on the derived amino acid level. One of them, PtCK2α3, has been expressed in Escherichia coli and characterized in vitro. As we also have observed with the isolated CK, the recombinant protein preferentially phosphorylates casein but also phosphorylates some Paramecium-specific substrates, including the exocytosis-sensitive phosphoprotein pp63/parafusin. Characteristically, Ca2+ inhibits the phosphorylation at elevated concentrations occurring during stimulation of a cell. Reconstitution with a recombinant form of the regulatory subunit from Xenopus laevis, XlCK2β, confirms Ca2+ sensitivity also under conditions of autophosphorylation. This is unusual for CK2 but correlates with the presence of two EF-hand calcium-binding motifs, one of which is located in the N-terminal segment essential for constitutive activity, as well as with an aberrant composition of normally basic domains recognizing acidic substrate domains. Immunogold localization reveals a considerable enrichment in the outermost cell cortex layers, excluding cilia. We discuss a potential role of this Ca2+-inhibited PtCK2α species in a late step of signal transduction.
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Barkova, Anastasia, Indranil Adhya, Christine Conesa, Amna Asif-Laidin, Amandine Bonnet, Elise Rabut, Carine Chagneau, Pascale Lesage, and Joël Acker. "A proteomic screen of Ty1 integrase partners identifies the protein kinase CK2 as a regulator of Ty1 retrotransposition." Mobile DNA 13, no. 1 (November 18, 2022). http://dx.doi.org/10.1186/s13100-022-00284-0.

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Abstract Background Transposable elements are ubiquitous and play a fundamental role in shaping genomes during evolution. Since excessive transposition can be mutagenic, mechanisms exist in the cells to keep these mobile elements under control. Although many cellular factors regulating the mobility of the retrovirus-like transposon Ty1 in Saccharomyces cerevisiae have been identified in genetic screens, only very few of them interact physically with Ty1 integrase (IN). Results Here, we perform a proteomic screen to establish Ty1 IN interactome. Among the 265 potential interacting partners, we focus our study on the conserved CK2 kinase. We confirm the interaction between IN and CK2, demonstrate that IN is a substrate of CK2 in vitro and identify the modified residues. We find that Ty1 IN is phosphorylated in vivo and that these modifications are dependent in part on CK2. No significant change in Ty1 retromobility could be observed when we introduce phospho-ablative mutations that prevent IN phosphorylation by CK2 in vitro. However, the absence of CK2 holoenzyme results in a strong stimulation of Ty1 retrotransposition, characterized by an increase in Ty1 mRNA and protein levels and a high accumulation of cDNA. Conclusion Our study shows that Ty1 IN is phosphorylated, as observed for retroviral INs and highlights an important role of CK2 in the regulation of Ty1 retrotransposition. In addition, the proteomic approach enabled the identification of many new Ty1 IN interacting partners, whose potential role in the control of Ty1 mobility will be interesting to study.
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Dissertations / Theses on the topic ""CK2,Substrate,Identification""

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khan, shahbaz. "Chemical genetic approach to identify substrates of CK2 kinase using Mass spectrometry." Doctoral thesis, 2018. http://hdl.handle.net/11562/978731.

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Protein kinase CK2 plays major roles in multiple biological processes, as has been reported in literature. Phosphoproteomic and bioinformatics data suggests that CK2 is involved in many cellular pathways however there is no report published on the unbiased global validation of its bona fine cellular substrates and how the CK2 dependent phosphorylation is modulating these pathways. Therefore, there is a need for methods that can do this validation process. Since the kinases have similar nature to phosphorylate their substrates, it is a great challenge to find or validate new substrates of a targeted kinase. In this study, a chemical genetics approach was used when the phenylalanine bulky residues were identified in CK2α as F113 and CK2α’ as F114. These residues were mutated to glycine to expand the ATP binding pocket, and create an analogues sensitive kinase which can utilize an ATP analogue nucleotide. The substitution did not alter the activity or specificity of the kinase. Furthermore, the analogue sensitive-CK2 (as-CK2) and wild type-CK2 (wt-CK2) α and α’ SILAC labeled stable cell lines were generated, then thiophosphrylation reactions were done using N6-(2-phenylethyl) ATPγS (2peATPγS) to label substrates in the cell lines. The thiopeptides were identified using mass spectrometry based proteomics approach. The thiopeptides found only in as-CK2 compared to control were considered as CK2 substrates. Our results highlight the potential of using analog-sensitive CK2 to further expand our knowledge of the cellular roles of CK2 and elucidate kinase-substrate relationships.
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