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Phospho‐regulation of mitotic spindle assembly
The assembly of the bipolar mitotic spindle requires the careful orchestration of a myriad of enzyme activities like protein posttranslational modifications. Among these, phosphorylation has arisen as the principle mode for spatially and temporally activating the proteins involved in early mitotic s...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley & Sons, Inc.
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7898546/ https://www.ncbi.nlm.nih.gov/pubmed/33280275 http://dx.doi.org/10.1002/cm.21649 |
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author | Ong, Joseph Y. Bradley, Michelle C. Torres, Jorge Z. |
author_facet | Ong, Joseph Y. Bradley, Michelle C. Torres, Jorge Z. |
author_sort | Ong, Joseph Y. |
collection | PubMed |
description | The assembly of the bipolar mitotic spindle requires the careful orchestration of a myriad of enzyme activities like protein posttranslational modifications. Among these, phosphorylation has arisen as the principle mode for spatially and temporally activating the proteins involved in early mitotic spindle assembly processes. Here, we review key kinases, phosphatases, and phosphorylation events that regulate critical aspects of these processes. We highlight key phosphorylation substrates that are important for ensuring the fidelity of centriole duplication, centrosome maturation, and the establishment of the bipolar spindle. We also highlight techniques used to understand kinase–substrate relationships and to study phosphorylation events. We conclude with perspectives on the field of posttranslational modifications in early mitotic spindle assembly. |
format | Online Article Text |
id | pubmed-7898546 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | John Wiley & Sons, Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-78985462021-03-03 Phospho‐regulation of mitotic spindle assembly Ong, Joseph Y. Bradley, Michelle C. Torres, Jorge Z. Cytoskeleton (Hoboken) Review Article The assembly of the bipolar mitotic spindle requires the careful orchestration of a myriad of enzyme activities like protein posttranslational modifications. Among these, phosphorylation has arisen as the principle mode for spatially and temporally activating the proteins involved in early mitotic spindle assembly processes. Here, we review key kinases, phosphatases, and phosphorylation events that regulate critical aspects of these processes. We highlight key phosphorylation substrates that are important for ensuring the fidelity of centriole duplication, centrosome maturation, and the establishment of the bipolar spindle. We also highlight techniques used to understand kinase–substrate relationships and to study phosphorylation events. We conclude with perspectives on the field of posttranslational modifications in early mitotic spindle assembly. John Wiley & Sons, Inc. 2020-12-16 2020-12 /pmc/articles/PMC7898546/ /pubmed/33280275 http://dx.doi.org/10.1002/cm.21649 Text en © 2020 The Authors. Cytoskeleton published by Wiley Periodicals LLC. This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes. |
spellingShingle | Review Article Ong, Joseph Y. Bradley, Michelle C. Torres, Jorge Z. Phospho‐regulation of mitotic spindle assembly |
title | Phospho‐regulation of mitotic spindle assembly |
title_full | Phospho‐regulation of mitotic spindle assembly |
title_fullStr | Phospho‐regulation of mitotic spindle assembly |
title_full_unstemmed | Phospho‐regulation of mitotic spindle assembly |
title_short | Phospho‐regulation of mitotic spindle assembly |
title_sort | phospho‐regulation of mitotic spindle assembly |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7898546/ https://www.ncbi.nlm.nih.gov/pubmed/33280275 http://dx.doi.org/10.1002/cm.21649 |
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