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CDK1-mediated CENP-C phosphorylation modulates CENP-A binding and mitotic kinetochore localization

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, direct...

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Autores principales: Watanabe, Reito, Hara, Masatoshi, Okumura, Ei-ichi, Hervé, Solène, Fachinetti, Daniele, Ariyoshi, Mariko, Fukagawa, Tatsuo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Rockefeller University Press 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6891089/
https://www.ncbi.nlm.nih.gov/pubmed/31676716
http://dx.doi.org/10.1083/jcb.201907006
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author Watanabe, Reito
Hara, Masatoshi
Okumura, Ei-ichi
Hervé, Solène
Fachinetti, Daniele
Ariyoshi, Mariko
Fukagawa, Tatsuo
author_facet Watanabe, Reito
Hara, Masatoshi
Okumura, Ei-ichi
Hervé, Solène
Fachinetti, Daniele
Ariyoshi, Mariko
Fukagawa, Tatsuo
author_sort Watanabe, Reito
collection PubMed
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.
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spelling pubmed-68910892020-06-02 CDK1-mediated CENP-C phosphorylation modulates CENP-A binding and mitotic kinetochore localization Watanabe, Reito Hara, Masatoshi Okumura, Ei-ichi Hervé, Solène Fachinetti, Daniele Ariyoshi, Mariko Fukagawa, Tatsuo J Cell Biol Research Articles 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. Rockefeller University Press 2019-12-02 2019-11-01 /pmc/articles/PMC6891089/ /pubmed/31676716 http://dx.doi.org/10.1083/jcb.201907006 Text en © 2019 Watanabe et al. http://www.rupress.org/terms/https://creativecommons.org/licenses/by-nc-sa/4.0/This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Research Articles
Watanabe, Reito
Hara, Masatoshi
Okumura, Ei-ichi
Hervé, Solène
Fachinetti, Daniele
Ariyoshi, Mariko
Fukagawa, Tatsuo
CDK1-mediated CENP-C phosphorylation modulates CENP-A binding and mitotic kinetochore localization
title CDK1-mediated CENP-C phosphorylation modulates CENP-A binding and mitotic kinetochore localization
title_full CDK1-mediated CENP-C phosphorylation modulates CENP-A binding and mitotic kinetochore localization
title_fullStr CDK1-mediated CENP-C phosphorylation modulates CENP-A binding and mitotic kinetochore localization
title_full_unstemmed CDK1-mediated CENP-C phosphorylation modulates CENP-A binding and mitotic kinetochore localization
title_short CDK1-mediated CENP-C phosphorylation modulates CENP-A binding and mitotic kinetochore localization
title_sort cdk1-mediated cenp-c phosphorylation modulates cenp-a binding and mitotic kinetochore localization
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6891089/
https://www.ncbi.nlm.nih.gov/pubmed/31676716
http://dx.doi.org/10.1083/jcb.201907006
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