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Myosin 1 controls membrane shape by coupling F-Actin to membrane
Cellular functions are intimately associated with rapid changes in membrane shape. Different mechanisms interfering with the lipid bilayer, such as the insertion of proteins with amphipatic helices or the association of a protein scaffold, trigger membrane bending. By exerting force on membranes, mo...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Landes Bioscience
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3384575/ https://www.ncbi.nlm.nih.gov/pubmed/22754614 http://dx.doi.org/10.4161/bioa.18406 |
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author | Coudrier, Evelyne Almeida, Claudia G. |
author_facet | Coudrier, Evelyne Almeida, Claudia G. |
author_sort | Coudrier, Evelyne |
collection | PubMed |
description | Cellular functions are intimately associated with rapid changes in membrane shape. Different mechanisms interfering with the lipid bilayer, such as the insertion of proteins with amphipatic helices or the association of a protein scaffold, trigger membrane bending. By exerting force on membranes, molecular motors can also contribute to membrane remodeling. Previous studies have shown that actin and myosin 1 participate in the invagination of the plasma membrane during endocytosis while kinesins and dynein with microtubules provide the force to elongate membrane buds at recycling endosomes and at the trans-Golgi network (TGN). Using live cell imaging we have recently shown that a myosin 1 (myosin 1b) regulates the actin dependent post-Golgi traffic of cargo and generates force that controls the assembly of F-actin foci and promotes with the actin cytoskeleton the formation of tubules at the TGN. Our data provide evidence that actin and myosin 1 can regulate membrane remodeling of organelles as well as having an unexpected role in the spatial organization of the actin cytoskeleton. Here, we discuss our results together with the role of actin and other myosins that have been implicated in the traffic of cargo. |
format | Online Article Text |
id | pubmed-3384575 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Landes Bioscience |
record_format | MEDLINE/PubMed |
spelling | pubmed-33845752012-06-29 Myosin 1 controls membrane shape by coupling F-Actin to membrane Coudrier, Evelyne Almeida, Claudia G. Bioarchitecture Perspective Cellular functions are intimately associated with rapid changes in membrane shape. Different mechanisms interfering with the lipid bilayer, such as the insertion of proteins with amphipatic helices or the association of a protein scaffold, trigger membrane bending. By exerting force on membranes, molecular motors can also contribute to membrane remodeling. Previous studies have shown that actin and myosin 1 participate in the invagination of the plasma membrane during endocytosis while kinesins and dynein with microtubules provide the force to elongate membrane buds at recycling endosomes and at the trans-Golgi network (TGN). Using live cell imaging we have recently shown that a myosin 1 (myosin 1b) regulates the actin dependent post-Golgi traffic of cargo and generates force that controls the assembly of F-actin foci and promotes with the actin cytoskeleton the formation of tubules at the TGN. Our data provide evidence that actin and myosin 1 can regulate membrane remodeling of organelles as well as having an unexpected role in the spatial organization of the actin cytoskeleton. Here, we discuss our results together with the role of actin and other myosins that have been implicated in the traffic of cargo. Landes Bioscience 2011-09-01 /pmc/articles/PMC3384575/ /pubmed/22754614 http://dx.doi.org/10.4161/bioa.18406 Text en Copyright © 2011 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited. |
spellingShingle | Perspective Coudrier, Evelyne Almeida, Claudia G. Myosin 1 controls membrane shape by coupling F-Actin to membrane |
title | Myosin 1 controls membrane shape by coupling F-Actin to membrane |
title_full | Myosin 1 controls membrane shape by coupling F-Actin to membrane |
title_fullStr | Myosin 1 controls membrane shape by coupling F-Actin to membrane |
title_full_unstemmed | Myosin 1 controls membrane shape by coupling F-Actin to membrane |
title_short | Myosin 1 controls membrane shape by coupling F-Actin to membrane |
title_sort | myosin 1 controls membrane shape by coupling f-actin to membrane |
topic | Perspective |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3384575/ https://www.ncbi.nlm.nih.gov/pubmed/22754614 http://dx.doi.org/10.4161/bioa.18406 |
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