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Coupled myosin VI motors facilitate unidirectional movement on an F-actin network
Unconventional myosins interact with the dense cortical actin network during processes such as membrane trafficking, cell migration, and mechanotransduction. Our understanding of unconventional myosin function is derived largely from assays that examine the interaction of a single myosin with a sing...
Autores principales: | , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2009
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2762089/ https://www.ncbi.nlm.nih.gov/pubmed/19786577 http://dx.doi.org/10.1083/jcb.200906133 |
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author | Sivaramakrishnan, Sivaraj Spudich, James A. |
author_facet | Sivaramakrishnan, Sivaraj Spudich, James A. |
author_sort | Sivaramakrishnan, Sivaraj |
collection | PubMed |
description | Unconventional myosins interact with the dense cortical actin network during processes such as membrane trafficking, cell migration, and mechanotransduction. Our understanding of unconventional myosin function is derived largely from assays that examine the interaction of a single myosin with a single actin filament. In this study, we have developed a model system to study the interaction between multiple tethered unconventional myosins and a model F-actin cortex, namely the lamellipodium of a migrating fish epidermal keratocyte. Using myosin VI, which moves toward the pointed end of actin filaments, we directly determine the polarity of the extracted keratocyte lamellipodium from the cell periphery to the cell nucleus. We use a combination of experimentation and simulation to demonstrate that multiple myosin VI molecules can coordinate to efficiently transport vesicle-size cargo over 10 µm of the dense interlaced actin network. Furthermore, several molecules of monomeric myosin VI, which are nonprocessive in single molecule assays, can coordinate to transport cargo with similar speeds as dimers. |
format | Text |
id | pubmed-2762089 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-27620892010-04-05 Coupled myosin VI motors facilitate unidirectional movement on an F-actin network Sivaramakrishnan, Sivaraj Spudich, James A. J Cell Biol Research Articles Unconventional myosins interact with the dense cortical actin network during processes such as membrane trafficking, cell migration, and mechanotransduction. Our understanding of unconventional myosin function is derived largely from assays that examine the interaction of a single myosin with a single actin filament. In this study, we have developed a model system to study the interaction between multiple tethered unconventional myosins and a model F-actin cortex, namely the lamellipodium of a migrating fish epidermal keratocyte. Using myosin VI, which moves toward the pointed end of actin filaments, we directly determine the polarity of the extracted keratocyte lamellipodium from the cell periphery to the cell nucleus. We use a combination of experimentation and simulation to demonstrate that multiple myosin VI molecules can coordinate to efficiently transport vesicle-size cargo over 10 µm of the dense interlaced actin network. Furthermore, several molecules of monomeric myosin VI, which are nonprocessive in single molecule assays, can coordinate to transport cargo with similar speeds as dimers. The Rockefeller University Press 2009-10-05 /pmc/articles/PMC2762089/ /pubmed/19786577 http://dx.doi.org/10.1083/jcb.200906133 Text en © 2009 Sivaramakrishnan and Spudich 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.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Research Articles Sivaramakrishnan, Sivaraj Spudich, James A. Coupled myosin VI motors facilitate unidirectional movement on an F-actin network |
title | Coupled myosin VI motors facilitate unidirectional movement on an F-actin network |
title_full | Coupled myosin VI motors facilitate unidirectional movement on an F-actin network |
title_fullStr | Coupled myosin VI motors facilitate unidirectional movement on an F-actin network |
title_full_unstemmed | Coupled myosin VI motors facilitate unidirectional movement on an F-actin network |
title_short | Coupled myosin VI motors facilitate unidirectional movement on an F-actin network |
title_sort | coupled myosin vi motors facilitate unidirectional movement on an f-actin network |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2762089/ https://www.ncbi.nlm.nih.gov/pubmed/19786577 http://dx.doi.org/10.1083/jcb.200906133 |
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