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Interplay between Phosphatases and the Anaphase-Promoting Complex/Cyclosome in Mitosis

Accurate division of cells into two daughters is a process that is vital to propagation of life. Protein phosphorylation and selective degradation have emerged as two important mechanisms safeguarding the delicate choreography of mitosis. Protein phosphatases catalyze dephosphorylation of thousands...

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Autores principales: Kataria, Meghna, Yamano, Hiroyuki
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6721574/
https://www.ncbi.nlm.nih.gov/pubmed/31382469
http://dx.doi.org/10.3390/cells8080814
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author Kataria, Meghna
Yamano, Hiroyuki
author_facet Kataria, Meghna
Yamano, Hiroyuki
author_sort Kataria, Meghna
collection PubMed
description Accurate division of cells into two daughters is a process that is vital to propagation of life. Protein phosphorylation and selective degradation have emerged as two important mechanisms safeguarding the delicate choreography of mitosis. Protein phosphatases catalyze dephosphorylation of thousands of sites on proteins, steering the cells through establishment of the mitotic phase and exit from it. A large E3 ubiquitin ligase, the anaphase-promoting complex/cyclosome (APC/C) becomes active during latter stages of mitosis through G1 and marks hundreds of proteins for destruction. Recent studies have revealed the complex interregulation between these two classes of enzymes. In this review, we highlight the direct and indirect mechanisms by which phosphatases and the APC/C mutually influence each other to ensure accurate spatiotemporal and orderly progression through mitosis, with a particular focus on recent insights and conceptual advances.
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spelling pubmed-67215742019-09-10 Interplay between Phosphatases and the Anaphase-Promoting Complex/Cyclosome in Mitosis Kataria, Meghna Yamano, Hiroyuki Cells Review Accurate division of cells into two daughters is a process that is vital to propagation of life. Protein phosphorylation and selective degradation have emerged as two important mechanisms safeguarding the delicate choreography of mitosis. Protein phosphatases catalyze dephosphorylation of thousands of sites on proteins, steering the cells through establishment of the mitotic phase and exit from it. A large E3 ubiquitin ligase, the anaphase-promoting complex/cyclosome (APC/C) becomes active during latter stages of mitosis through G1 and marks hundreds of proteins for destruction. Recent studies have revealed the complex interregulation between these two classes of enzymes. In this review, we highlight the direct and indirect mechanisms by which phosphatases and the APC/C mutually influence each other to ensure accurate spatiotemporal and orderly progression through mitosis, with a particular focus on recent insights and conceptual advances. MDPI 2019-08-02 /pmc/articles/PMC6721574/ /pubmed/31382469 http://dx.doi.org/10.3390/cells8080814 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Kataria, Meghna
Yamano, Hiroyuki
Interplay between Phosphatases and the Anaphase-Promoting Complex/Cyclosome in Mitosis
title Interplay between Phosphatases and the Anaphase-Promoting Complex/Cyclosome in Mitosis
title_full Interplay between Phosphatases and the Anaphase-Promoting Complex/Cyclosome in Mitosis
title_fullStr Interplay between Phosphatases and the Anaphase-Promoting Complex/Cyclosome in Mitosis
title_full_unstemmed Interplay between Phosphatases and the Anaphase-Promoting Complex/Cyclosome in Mitosis
title_short Interplay between Phosphatases and the Anaphase-Promoting Complex/Cyclosome in Mitosis
title_sort interplay between phosphatases and the anaphase-promoting complex/cyclosome in mitosis
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6721574/
https://www.ncbi.nlm.nih.gov/pubmed/31382469
http://dx.doi.org/10.3390/cells8080814
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