Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Sivaramakrishnan, Sivaraj, Spudich, James A.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2009
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
_version_ 1782172894529323008
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
work_keys_str_mv AT sivaramakrishnansivaraj coupledmyosinvimotorsfacilitateunidirectionalmovementonanfactinnetwork
AT spudichjamesa coupledmyosinvimotorsfacilitateunidirectionalmovementonanfactinnetwork