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Ctf3/CENP-I provides a docking site for the desumoylase Ulp2 at the kinetochore
The step-by-step process of chromosome segregation defines the stages of the cell cycle. In eukaryotes, signals controlling these steps converge upon the kinetochore, a multiprotein assembly that connects spindle microtubules to chromosomal centromeres. Kinetochores control and adapt to major chromo...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Rockefeller University Press
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8178754/ https://www.ncbi.nlm.nih.gov/pubmed/34081091 http://dx.doi.org/10.1083/jcb.202012149 |
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author | Quan, Yun Hinshaw, Stephen M. Wang, Pang-Che Harrison, Stephen C. Zhou, Huilin |
author_facet | Quan, Yun Hinshaw, Stephen M. Wang, Pang-Che Harrison, Stephen C. Zhou, Huilin |
author_sort | Quan, Yun |
collection | PubMed |
description | The step-by-step process of chromosome segregation defines the stages of the cell cycle. In eukaryotes, signals controlling these steps converge upon the kinetochore, a multiprotein assembly that connects spindle microtubules to chromosomal centromeres. Kinetochores control and adapt to major chromosomal transactions, including replication of centromeric DNA, biorientation of sister centromeres on the metaphase spindle, and transit of sister chromatids into daughter cells during anaphase. Although the mechanisms that ensure tight microtubule coupling at anaphase are at least partly understood, kinetochore adaptations that support other cell cycle transitions are not. We report here a mechanism that enables regulated control of kinetochore sumoylation. A conserved surface of the Ctf3/CENP-I kinetochore protein provides a binding site for Ulp2, the nuclear enzyme that removes SUMO chains from modified substrates. Ctf3 mutations that disable Ulp2 recruitment cause elevated inner kinetochore sumoylation and defective chromosome segregation. The location of the site within the assembled kinetochore suggests coordination between sumoylation and other cell cycle–regulated processes. |
format | Online Article Text |
id | pubmed-8178754 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-81787542022-02-02 Ctf3/CENP-I provides a docking site for the desumoylase Ulp2 at the kinetochore Quan, Yun Hinshaw, Stephen M. Wang, Pang-Che Harrison, Stephen C. Zhou, Huilin J Cell Biol Article The step-by-step process of chromosome segregation defines the stages of the cell cycle. In eukaryotes, signals controlling these steps converge upon the kinetochore, a multiprotein assembly that connects spindle microtubules to chromosomal centromeres. Kinetochores control and adapt to major chromosomal transactions, including replication of centromeric DNA, biorientation of sister centromeres on the metaphase spindle, and transit of sister chromatids into daughter cells during anaphase. Although the mechanisms that ensure tight microtubule coupling at anaphase are at least partly understood, kinetochore adaptations that support other cell cycle transitions are not. We report here a mechanism that enables regulated control of kinetochore sumoylation. A conserved surface of the Ctf3/CENP-I kinetochore protein provides a binding site for Ulp2, the nuclear enzyme that removes SUMO chains from modified substrates. Ctf3 mutations that disable Ulp2 recruitment cause elevated inner kinetochore sumoylation and defective chromosome segregation. The location of the site within the assembled kinetochore suggests coordination between sumoylation and other cell cycle–regulated processes. Rockefeller University Press 2021-06-03 /pmc/articles/PMC8178754/ /pubmed/34081091 http://dx.doi.org/10.1083/jcb.202012149 Text en © 2021 Quan 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 | Article Quan, Yun Hinshaw, Stephen M. Wang, Pang-Che Harrison, Stephen C. Zhou, Huilin Ctf3/CENP-I provides a docking site for the desumoylase Ulp2 at the kinetochore |
title | Ctf3/CENP-I provides a docking site for the desumoylase Ulp2 at the kinetochore |
title_full | Ctf3/CENP-I provides a docking site for the desumoylase Ulp2 at the kinetochore |
title_fullStr | Ctf3/CENP-I provides a docking site for the desumoylase Ulp2 at the kinetochore |
title_full_unstemmed | Ctf3/CENP-I provides a docking site for the desumoylase Ulp2 at the kinetochore |
title_short | Ctf3/CENP-I provides a docking site for the desumoylase Ulp2 at the kinetochore |
title_sort | ctf3/cenp-i provides a docking site for the desumoylase ulp2 at the kinetochore |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8178754/ https://www.ncbi.nlm.nih.gov/pubmed/34081091 http://dx.doi.org/10.1083/jcb.202012149 |
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