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Direct observation of the conformational states of formin mDia1 at actin filament barbed ends and along the filament
The fine regulation of actin polymerization is essential to control cell motility and architecture and to perform essential cellular functions. Formins are key regulators of actin filament assembly, known to processively elongate filament barbed ends and increase their polymerization rate. Different...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9816646/ https://www.ncbi.nlm.nih.gov/pubmed/36383775 http://dx.doi.org/10.1091/mbc.E22-10-0472 |
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author | Maufront, Julien Guichard, Bérengère Cao, Lu-Yan Cicco, Aurélie Di Jégou, Antoine Romet-Lemonne, Guillaume Bertin, Aurélie |
author_facet | Maufront, Julien Guichard, Bérengère Cao, Lu-Yan Cicco, Aurélie Di Jégou, Antoine Romet-Lemonne, Guillaume Bertin, Aurélie |
author_sort | Maufront, Julien |
collection | PubMed |
description | The fine regulation of actin polymerization is essential to control cell motility and architecture and to perform essential cellular functions. Formins are key regulators of actin filament assembly, known to processively elongate filament barbed ends and increase their polymerization rate. Different models have been extrapolated to describe the molecular mechanism governing the processive motion of formin FH2 domains at polymerizing barbed ends. Using negative stain electron microscopy, we directly identified for the first time two conformations of the mDia1 formin FH2 domains in interaction with the barbed ends of actin filaments. These conformations agree with the speculated open and closed conformations of the “stair-stepping” model. We observed the FH2 dimers to be in the open conformation for 79% of the data, interacting with the two terminal actin subunits of the barbed end while they interact with three actin subunits in the closed conformation. In addition, we identified and characterized the structure of single FH2 dimers encircling the core of actin filaments, and reveal their ability to spontaneously depart from barbed ends. |
format | Online Article Text |
id | pubmed-9816646 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-98166462023-01-19 Direct observation of the conformational states of formin mDia1 at actin filament barbed ends and along the filament Maufront, Julien Guichard, Bérengère Cao, Lu-Yan Cicco, Aurélie Di Jégou, Antoine Romet-Lemonne, Guillaume Bertin, Aurélie Mol Biol Cell Articles The fine regulation of actin polymerization is essential to control cell motility and architecture and to perform essential cellular functions. Formins are key regulators of actin filament assembly, known to processively elongate filament barbed ends and increase their polymerization rate. Different models have been extrapolated to describe the molecular mechanism governing the processive motion of formin FH2 domains at polymerizing barbed ends. Using negative stain electron microscopy, we directly identified for the first time two conformations of the mDia1 formin FH2 domains in interaction with the barbed ends of actin filaments. These conformations agree with the speculated open and closed conformations of the “stair-stepping” model. We observed the FH2 dimers to be in the open conformation for 79% of the data, interacting with the two terminal actin subunits of the barbed end while they interact with three actin subunits in the closed conformation. In addition, we identified and characterized the structure of single FH2 dimers encircling the core of actin filaments, and reveal their ability to spontaneously depart from barbed ends. The American Society for Cell Biology 2022-12-15 /pmc/articles/PMC9816646/ /pubmed/36383775 http://dx.doi.org/10.1091/mbc.E22-10-0472 Text en © 2023 Maufront et al. “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. https://creativecommons.org/licenses/by/4.0/This article is distributed by The American Society for Cell Biology under license from the author(s). It is available to the public under an Attribution 4.0 International Creative Commons CC-BY 4.0 License. |
spellingShingle | Articles Maufront, Julien Guichard, Bérengère Cao, Lu-Yan Cicco, Aurélie Di Jégou, Antoine Romet-Lemonne, Guillaume Bertin, Aurélie Direct observation of the conformational states of formin mDia1 at actin filament barbed ends and along the filament |
title | Direct observation of the conformational states of formin mDia1 at actin filament barbed ends and along the filament |
title_full | Direct observation of the conformational states of formin mDia1 at actin filament barbed ends and along the filament |
title_fullStr | Direct observation of the conformational states of formin mDia1 at actin filament barbed ends and along the filament |
title_full_unstemmed | Direct observation of the conformational states of formin mDia1 at actin filament barbed ends and along the filament |
title_short | Direct observation of the conformational states of formin mDia1 at actin filament barbed ends and along the filament |
title_sort | direct observation of the conformational states of formin mdia1 at actin filament barbed ends and along the filament |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9816646/ https://www.ncbi.nlm.nih.gov/pubmed/36383775 http://dx.doi.org/10.1091/mbc.E22-10-0472 |
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