{"database":"biostudies-literature","file_versions":[],"scores":{"citationCount":0,"reanalysisCount":0,"viewCount":66,"searchCount":0},"additional":{"omics_type":["Unknown"],"volume":["218(12)"],"submitter":["Watanabe R"],"pubmed_abstract":["The kinetochore is essential for faithful chromosome segregation during mitosis. To form a functional kinetochore, constitutive centromere-associated network (CCAN) proteins are assembled on the centromere chromatin that contains the centromere-specific histone CENP-A. CENP-C, a CCAN protein, directly interacts with the CENP-A nucleosome to nucleate the kinetochore structure. As CENP-C is a hub protein for kinetochore assembly, it is critical to address how the CENP-A-CENP-C interaction is regulated during cell cycle progression. To address this question, we investigated the CENP-C C-terminal region, including a conserved CENP-A-binding motif, in both chicken and human cells and found that CDK1-mediated phosphorylation of CENP-C facilitates its binding to CENP-A in vitro and in vivo. We observed that CENP-A binding is involved in CENP-C kinetochore localization during mitosis. We also demonstrate that the CENP-A-CENP-C interaction is critical for long-term viability in human RPE-1 cells. These results provide deeper insights into protein-interaction network plasticity in centromere proteins during cell cycle progression."],"journal":["The Journal of cell biology"],"pagination":["4042-4062"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6891089"],"repository":["biostudies-literature"],"pubmed_title":["CDK1-mediated CENP-C phosphorylation modulates CENP-A binding and mitotic kinetochore localization."],"pmcid":["PMC6891089"],"pubmed_authors":["Herve S","Fachinetti D","Ariyoshi M","Fukagawa T","Okumura EI","Hara M","Watanabe R"],"view_count":["66"],"additional_accession":[]},"is_claimable":false,"name":"CDK1-mediated CENP-C phosphorylation modulates CENP-A binding and mitotic kinetochore localization.","description":"The kinetochore is essential for faithful chromosome segregation during mitosis. To form a functional kinetochore, constitutive centromere-associated network (CCAN) proteins are assembled on the centromere chromatin that contains the centromere-specific histone CENP-A. CENP-C, a CCAN protein, directly interacts with the CENP-A nucleosome to nucleate the kinetochore structure. As CENP-C is a hub protein for kinetochore assembly, it is critical to address how the CENP-A-CENP-C interaction is regulated during cell cycle progression. To address this question, we investigated the CENP-C C-terminal region, including a conserved CENP-A-binding motif, in both chicken and human cells and found that CDK1-mediated phosphorylation of CENP-C facilitates its binding to CENP-A in vitro and in vivo. We observed that CENP-A binding is involved in CENP-C kinetochore localization during mitosis. We also demonstrate that the CENP-A-CENP-C interaction is critical for long-term viability in human RPE-1 cells. These results provide deeper insights into protein-interaction network plasticity in centromere proteins during cell cycle progression.","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Dec","modification":"2020-06-05T07:00:30Z","creation":"2020-06-05T07:00:30Z"},"accession":"S-EPMC6891089","cross_references":{"pubmed":["31676716"],"doi":["10.1083/jcb.201907006 "]}}