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Emerging roles of the SUMO pathway in mitosis
SUMO proteins are small ubiquitin-like modifiers found in all eukaryotes that become covalently conjugated to other cellular proteins. The SUMO conjugation pathway is biochemically similar to ubiquitin conjugation, although the enzymes within the pathway act exclusively on SUMO proteins. This post-t...
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2008
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2265688/ https://www.ncbi.nlm.nih.gov/pubmed/18218095 http://dx.doi.org/10.1186/1747-1028-3-5 |
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author | Dasso, Mary |
author_facet | Dasso, Mary |
author_sort | Dasso, Mary |
collection | PubMed |
description | SUMO proteins are small ubiquitin-like modifiers found in all eukaryotes that become covalently conjugated to other cellular proteins. The SUMO conjugation pathway is biochemically similar to ubiquitin conjugation, although the enzymes within the pathway act exclusively on SUMO proteins. This post-translational modification controls many processes. Here, I will focus on evidence that SUMOylation plays a critical role(s) in mitosis: Early studies showed a genetic requirement for SUMO pathway components in the process of cell division, while later findings implicated SUMOylation in the control of mitotic chromosome structure, cell cycle progression, kinetochore function and cytokinesis. Recent insights into the targets of SUMOylation are likely to be extremely helpful in understanding each of these aspects. Finally, growing evidence suggests that SUMOylation is a downstream target of regulation through Ran, a small GTPase with important functions in both interphase nuclear trafficking and mitotic spindle assembly. |
format | Text |
id | pubmed-2265688 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-22656882008-03-08 Emerging roles of the SUMO pathway in mitosis Dasso, Mary Cell Div Review SUMO proteins are small ubiquitin-like modifiers found in all eukaryotes that become covalently conjugated to other cellular proteins. The SUMO conjugation pathway is biochemically similar to ubiquitin conjugation, although the enzymes within the pathway act exclusively on SUMO proteins. This post-translational modification controls many processes. Here, I will focus on evidence that SUMOylation plays a critical role(s) in mitosis: Early studies showed a genetic requirement for SUMO pathway components in the process of cell division, while later findings implicated SUMOylation in the control of mitotic chromosome structure, cell cycle progression, kinetochore function and cytokinesis. Recent insights into the targets of SUMOylation are likely to be extremely helpful in understanding each of these aspects. Finally, growing evidence suggests that SUMOylation is a downstream target of regulation through Ran, a small GTPase with important functions in both interphase nuclear trafficking and mitotic spindle assembly. BioMed Central 2008-01-24 /pmc/articles/PMC2265688/ /pubmed/18218095 http://dx.doi.org/10.1186/1747-1028-3-5 Text en Copyright © 2008 Dasso; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Dasso, Mary Emerging roles of the SUMO pathway in mitosis |
title | Emerging roles of the SUMO pathway in mitosis |
title_full | Emerging roles of the SUMO pathway in mitosis |
title_fullStr | Emerging roles of the SUMO pathway in mitosis |
title_full_unstemmed | Emerging roles of the SUMO pathway in mitosis |
title_short | Emerging roles of the SUMO pathway in mitosis |
title_sort | emerging roles of the sumo pathway in mitosis |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2265688/ https://www.ncbi.nlm.nih.gov/pubmed/18218095 http://dx.doi.org/10.1186/1747-1028-3-5 |
work_keys_str_mv | AT dassomary emergingrolesofthesumopathwayinmitosis |