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SUMOylation of human septins is critical for septin filament bundling and cytokinesis

Septins are cytoskeletal proteins that assemble into nonpolar filaments. They are critical in diverse cellular functions, acting as scaffolds for protein recruitment and as diffusion barriers for subcellular compartmentalization. Human septins are encoded by 13 different genes and are classified int...

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Autores principales: Ribet, David, Boscaini, Serena, Cauvin, Clothilde, Siguier, Martin, Mostowy, Serge, Echard, Arnaud, Cossart, Pascale
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5716278/
https://www.ncbi.nlm.nih.gov/pubmed/29051266
http://dx.doi.org/10.1083/jcb.201703096
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author Ribet, David
Boscaini, Serena
Cauvin, Clothilde
Siguier, Martin
Mostowy, Serge
Echard, Arnaud
Cossart, Pascale
author_facet Ribet, David
Boscaini, Serena
Cauvin, Clothilde
Siguier, Martin
Mostowy, Serge
Echard, Arnaud
Cossart, Pascale
author_sort Ribet, David
collection PubMed
description Septins are cytoskeletal proteins that assemble into nonpolar filaments. They are critical in diverse cellular functions, acting as scaffolds for protein recruitment and as diffusion barriers for subcellular compartmentalization. Human septins are encoded by 13 different genes and are classified into four groups based on sequence homology (SEPT2, SEPT3, SEPT6, and SEPT7 groups). In yeast, septins were among the first proteins reported to be modified by SUMOylation, a ubiquitin-like posttranslational modification. However, whether human septins could be modified by small ubiquitin-like modifiers (SUMOs) and what roles this modification may have in septin function remains unknown. In this study, we first show that septins from all four human septin groups can be covalently modified by SUMOs. We show in particular that endogenous SEPT7 is constitutively SUMOylated during the cell cycle. We then map SUMOylation sites to the C-terminal domain of septins belonging to the SEPT6 and SEPT7 groups and to the N-terminal domain of septins from the SEPT3 group. We finally demonstrate that expression of non-SUMOylatable septin variants from the SEPT6 and SEPT7 groups leads to aberrant septin bundle formation and defects in cytokinesis after furrow ingression. Altogether, our results demonstrate a pivotal role for SUMOylation in septin filament bundling and cell division.
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spelling pubmed-57162782018-06-04 SUMOylation of human septins is critical for septin filament bundling and cytokinesis Ribet, David Boscaini, Serena Cauvin, Clothilde Siguier, Martin Mostowy, Serge Echard, Arnaud Cossart, Pascale J Cell Biol Research Articles Septins are cytoskeletal proteins that assemble into nonpolar filaments. They are critical in diverse cellular functions, acting as scaffolds for protein recruitment and as diffusion barriers for subcellular compartmentalization. Human septins are encoded by 13 different genes and are classified into four groups based on sequence homology (SEPT2, SEPT3, SEPT6, and SEPT7 groups). In yeast, septins were among the first proteins reported to be modified by SUMOylation, a ubiquitin-like posttranslational modification. However, whether human septins could be modified by small ubiquitin-like modifiers (SUMOs) and what roles this modification may have in septin function remains unknown. In this study, we first show that septins from all four human septin groups can be covalently modified by SUMOs. We show in particular that endogenous SEPT7 is constitutively SUMOylated during the cell cycle. We then map SUMOylation sites to the C-terminal domain of septins belonging to the SEPT6 and SEPT7 groups and to the N-terminal domain of septins from the SEPT3 group. We finally demonstrate that expression of non-SUMOylatable septin variants from the SEPT6 and SEPT7 groups leads to aberrant septin bundle formation and defects in cytokinesis after furrow ingression. Altogether, our results demonstrate a pivotal role for SUMOylation in septin filament bundling and cell division. The Rockefeller University Press 2017-12-04 /pmc/articles/PMC5716278/ /pubmed/29051266 http://dx.doi.org/10.1083/jcb.201703096 Text en © 2017 Ribet 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 Research Articles
Ribet, David
Boscaini, Serena
Cauvin, Clothilde
Siguier, Martin
Mostowy, Serge
Echard, Arnaud
Cossart, Pascale
SUMOylation of human septins is critical for septin filament bundling and cytokinesis
title SUMOylation of human septins is critical for septin filament bundling and cytokinesis
title_full SUMOylation of human septins is critical for septin filament bundling and cytokinesis
title_fullStr SUMOylation of human septins is critical for septin filament bundling and cytokinesis
title_full_unstemmed SUMOylation of human septins is critical for septin filament bundling and cytokinesis
title_short SUMOylation of human septins is critical for septin filament bundling and cytokinesis
title_sort sumoylation of human septins is critical for septin filament bundling and cytokinesis
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5716278/
https://www.ncbi.nlm.nih.gov/pubmed/29051266
http://dx.doi.org/10.1083/jcb.201703096
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