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Septins as membrane influencers: direct play or in association with other cytoskeleton partners

The cytoskeleton comprises three polymerizing structures that have been studied for a long time, actin microfilaments, microtubules and intermediate filaments, plus more recently investigated dynamic assemblies like septins or the endocytic-sorting complex required for transport (ESCRT) complex. The...

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Autores principales: Benoit, Béatrice, Poüs, Christian, Baillet, Anita
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9982393/
https://www.ncbi.nlm.nih.gov/pubmed/36875762
http://dx.doi.org/10.3389/fcell.2023.1112319
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author Benoit, Béatrice
Poüs, Christian
Baillet, Anita
author_facet Benoit, Béatrice
Poüs, Christian
Baillet, Anita
author_sort Benoit, Béatrice
collection PubMed
description The cytoskeleton comprises three polymerizing structures that have been studied for a long time, actin microfilaments, microtubules and intermediate filaments, plus more recently investigated dynamic assemblies like septins or the endocytic-sorting complex required for transport (ESCRT) complex. These filament-forming proteins control several cell functions through crosstalks with each other and with membranes. In this review, we report recent works that address how septins bind to membranes, and influence their shaping, organization, properties and functions, either by binding to them directly or indirectly through other cytoskeleton elements.
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spelling pubmed-99823932023-03-04 Septins as membrane influencers: direct play or in association with other cytoskeleton partners Benoit, Béatrice Poüs, Christian Baillet, Anita Front Cell Dev Biol Cell and Developmental Biology The cytoskeleton comprises three polymerizing structures that have been studied for a long time, actin microfilaments, microtubules and intermediate filaments, plus more recently investigated dynamic assemblies like septins or the endocytic-sorting complex required for transport (ESCRT) complex. These filament-forming proteins control several cell functions through crosstalks with each other and with membranes. In this review, we report recent works that address how septins bind to membranes, and influence their shaping, organization, properties and functions, either by binding to them directly or indirectly through other cytoskeleton elements. Frontiers Media S.A. 2023-02-17 /pmc/articles/PMC9982393/ /pubmed/36875762 http://dx.doi.org/10.3389/fcell.2023.1112319 Text en Copyright © 2023 Benoit, Poüs and Baillet. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Cell and Developmental Biology
Benoit, Béatrice
Poüs, Christian
Baillet, Anita
Septins as membrane influencers: direct play or in association with other cytoskeleton partners
title Septins as membrane influencers: direct play or in association with other cytoskeleton partners
title_full Septins as membrane influencers: direct play or in association with other cytoskeleton partners
title_fullStr Septins as membrane influencers: direct play or in association with other cytoskeleton partners
title_full_unstemmed Septins as membrane influencers: direct play or in association with other cytoskeleton partners
title_short Septins as membrane influencers: direct play or in association with other cytoskeleton partners
title_sort septins as membrane influencers: direct play or in association with other cytoskeleton partners
topic Cell and Developmental Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9982393/
https://www.ncbi.nlm.nih.gov/pubmed/36875762
http://dx.doi.org/10.3389/fcell.2023.1112319
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