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SUMOylation of nuclear actin
Actin, a major component of the cytoplasm, is also abundant in the nucleus. Nuclear actin is involved in a variety of nuclear processes including transcription, chromatin remodeling, and intranuclear transport. Nevertheless, the regulation of nuclear actin by posttranslational modifications has not...
Autores principales: | , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2009
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2717643/ https://www.ncbi.nlm.nih.gov/pubmed/19635839 http://dx.doi.org/10.1083/jcb.200905016 |
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author | Hofmann, Wilma A. Arduini, Alessandro Nicol, Samantha M. Camacho, Carlos J. Lessard, James L. Fuller-Pace, Frances V. de Lanerolle, Primal |
author_facet | Hofmann, Wilma A. Arduini, Alessandro Nicol, Samantha M. Camacho, Carlos J. Lessard, James L. Fuller-Pace, Frances V. de Lanerolle, Primal |
author_sort | Hofmann, Wilma A. |
collection | PubMed |
description | Actin, a major component of the cytoplasm, is also abundant in the nucleus. Nuclear actin is involved in a variety of nuclear processes including transcription, chromatin remodeling, and intranuclear transport. Nevertheless, the regulation of nuclear actin by posttranslational modifications has not been investigated. We now show that nuclear actin is modified by SUMO2 and SUMO3 and that computational modeling and site-directed mutagenesis identified K68 and K284 as critical sites for SUMOylating actin. We also present a model for the actin–SUMO complex and show that SUMOylation is required for the nuclear localization of actin. |
format | Text |
id | pubmed-2717643 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-27176432010-01-27 SUMOylation of nuclear actin Hofmann, Wilma A. Arduini, Alessandro Nicol, Samantha M. Camacho, Carlos J. Lessard, James L. Fuller-Pace, Frances V. de Lanerolle, Primal J Cell Biol Research Articles Actin, a major component of the cytoplasm, is also abundant in the nucleus. Nuclear actin is involved in a variety of nuclear processes including transcription, chromatin remodeling, and intranuclear transport. Nevertheless, the regulation of nuclear actin by posttranslational modifications has not been investigated. We now show that nuclear actin is modified by SUMO2 and SUMO3 and that computational modeling and site-directed mutagenesis identified K68 and K284 as critical sites for SUMOylating actin. We also present a model for the actin–SUMO complex and show that SUMOylation is required for the nuclear localization of actin. The Rockefeller University Press 2009-07-27 /pmc/articles/PMC2717643/ /pubmed/19635839 http://dx.doi.org/10.1083/jcb.200905016 Text en © 2009 Hofmann et al. 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.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Research Articles Hofmann, Wilma A. Arduini, Alessandro Nicol, Samantha M. Camacho, Carlos J. Lessard, James L. Fuller-Pace, Frances V. de Lanerolle, Primal SUMOylation of nuclear actin |
title | SUMOylation of nuclear actin |
title_full | SUMOylation of nuclear actin |
title_fullStr | SUMOylation of nuclear actin |
title_full_unstemmed | SUMOylation of nuclear actin |
title_short | SUMOylation of nuclear actin |
title_sort | sumoylation of nuclear actin |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2717643/ https://www.ncbi.nlm.nih.gov/pubmed/19635839 http://dx.doi.org/10.1083/jcb.200905016 |
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