Myosin 1b is an actin depolymerase

The regulation of actin dynamics is essential for various cellular processes. Former evidence suggests a correlation between the function of non-conventional myosin motors and actin dynamics. Here we investigate the contribution of myosin 1b to actin dynamics using sliding motility assays. We observ...

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Autores principales: Pernier, Julien, Kusters, Remy, Bousquet, Hugo, Lagny, Thibaut, Morchain, Antoine, Joanny, Jean-François, Bassereau, Patricia, Coudrier, Evelyne
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6858320/
https://www.ncbi.nlm.nih.gov/pubmed/31729365
http://dx.doi.org/10.1038/s41467-019-13160-y
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author Pernier, Julien
Kusters, Remy
Bousquet, Hugo
Lagny, Thibaut
Morchain, Antoine
Joanny, Jean-François
Bassereau, Patricia
Coudrier, Evelyne
author_facet Pernier, Julien
Kusters, Remy
Bousquet, Hugo
Lagny, Thibaut
Morchain, Antoine
Joanny, Jean-François
Bassereau, Patricia
Coudrier, Evelyne
author_sort Pernier, Julien
collection PubMed
description The regulation of actin dynamics is essential for various cellular processes. Former evidence suggests a correlation between the function of non-conventional myosin motors and actin dynamics. Here we investigate the contribution of myosin 1b to actin dynamics using sliding motility assays. We observe that sliding on myosin 1b immobilized or bound to a fluid bilayer enhances actin depolymerization at the barbed end, while sliding on myosin II, although 5 times faster, has no effect. This work reveals a non-conventional myosin motor as another type of depolymerase and points to its singular interactions with the actin barbed end.
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spelling pubmed-68583202019-11-20 Myosin 1b is an actin depolymerase Pernier, Julien Kusters, Remy Bousquet, Hugo Lagny, Thibaut Morchain, Antoine Joanny, Jean-François Bassereau, Patricia Coudrier, Evelyne Nat Commun Article The regulation of actin dynamics is essential for various cellular processes. Former evidence suggests a correlation between the function of non-conventional myosin motors and actin dynamics. Here we investigate the contribution of myosin 1b to actin dynamics using sliding motility assays. We observe that sliding on myosin 1b immobilized or bound to a fluid bilayer enhances actin depolymerization at the barbed end, while sliding on myosin II, although 5 times faster, has no effect. This work reveals a non-conventional myosin motor as another type of depolymerase and points to its singular interactions with the actin barbed end. Nature Publishing Group UK 2019-11-15 /pmc/articles/PMC6858320/ /pubmed/31729365 http://dx.doi.org/10.1038/s41467-019-13160-y Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Pernier, Julien
Kusters, Remy
Bousquet, Hugo
Lagny, Thibaut
Morchain, Antoine
Joanny, Jean-François
Bassereau, Patricia
Coudrier, Evelyne
Myosin 1b is an actin depolymerase
title Myosin 1b is an actin depolymerase
title_full Myosin 1b is an actin depolymerase
title_fullStr Myosin 1b is an actin depolymerase
title_full_unstemmed Myosin 1b is an actin depolymerase
title_short Myosin 1b is an actin depolymerase
title_sort myosin 1b is an actin depolymerase
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6858320/
https://www.ncbi.nlm.nih.gov/pubmed/31729365
http://dx.doi.org/10.1038/s41467-019-13160-y
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