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Targeting and transport: How microtubules control focal adhesion dynamics

Directional cell migration requires force generation that relies on the coordinated remodeling of interactions with the extracellular matrix (ECM), which is mediated by integrin-based focal adhesions (FAs). Normal FA turnover requires dynamic microtubules, and three members of the diverse group of m...

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Detalles Bibliográficos
Autores principales: Stehbens, Samantha, Wittmann, Torsten
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3514042/
https://www.ncbi.nlm.nih.gov/pubmed/22908306
http://dx.doi.org/10.1083/jcb.201206050
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author Stehbens, Samantha
Wittmann, Torsten
author_facet Stehbens, Samantha
Wittmann, Torsten
author_sort Stehbens, Samantha
collection PubMed
description Directional cell migration requires force generation that relies on the coordinated remodeling of interactions with the extracellular matrix (ECM), which is mediated by integrin-based focal adhesions (FAs). Normal FA turnover requires dynamic microtubules, and three members of the diverse group of microtubule plus-end-tracking proteins are principally involved in mediating microtubule interactions with FAs. Microtubules also alter the assembly state of FAs by modulating Rho GTPase signaling, and recent evidence suggests that microtubule-mediated clathrin-dependent and -independent endocytosis regulates FA dynamics. In addition, FA-associated microtubules may provide a polarized microtubule track for localized secretion of matrix metalloproteases (MMPs). Thus, different aspects of the molecular mechanisms by which microtubules control FA turnover in migrating cells are beginning to emerge.
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spelling pubmed-35140422013-02-20 Targeting and transport: How microtubules control focal adhesion dynamics Stehbens, Samantha Wittmann, Torsten J Cell Biol Reviews Directional cell migration requires force generation that relies on the coordinated remodeling of interactions with the extracellular matrix (ECM), which is mediated by integrin-based focal adhesions (FAs). Normal FA turnover requires dynamic microtubules, and three members of the diverse group of microtubule plus-end-tracking proteins are principally involved in mediating microtubule interactions with FAs. Microtubules also alter the assembly state of FAs by modulating Rho GTPase signaling, and recent evidence suggests that microtubule-mediated clathrin-dependent and -independent endocytosis regulates FA dynamics. In addition, FA-associated microtubules may provide a polarized microtubule track for localized secretion of matrix metalloproteases (MMPs). Thus, different aspects of the molecular mechanisms by which microtubules control FA turnover in migrating cells are beginning to emerge. The Rockefeller University Press 2012-08-20 /pmc/articles/PMC3514042/ /pubmed/22908306 http://dx.doi.org/10.1083/jcb.201206050 Text en © 2012 Stehbens and Wittmann 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.rupress.org/terms). 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 Reviews
Stehbens, Samantha
Wittmann, Torsten
Targeting and transport: How microtubules control focal adhesion dynamics
title Targeting and transport: How microtubules control focal adhesion dynamics
title_full Targeting and transport: How microtubules control focal adhesion dynamics
title_fullStr Targeting and transport: How microtubules control focal adhesion dynamics
title_full_unstemmed Targeting and transport: How microtubules control focal adhesion dynamics
title_short Targeting and transport: How microtubules control focal adhesion dynamics
title_sort targeting and transport: how microtubules control focal adhesion dynamics
topic Reviews
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3514042/
https://www.ncbi.nlm.nih.gov/pubmed/22908306
http://dx.doi.org/10.1083/jcb.201206050
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