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Talin Dependent Mechanosensitivity of Cell Focal Adhesions

A fundamental question in mechanobiology is how mechanical stimuli are sensed by mechanosensing proteins and converted into signals that direct cells to adapt to the external environment. A key function of cell adhesion to the extracellular matrix (ECM) is to transduce mechanical forces between cell...

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Detalles Bibliográficos
Autores principales: Yan, Jie, Yao, Mingxi, Goult, Benjamin T., Sheetz, Michael P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer US 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4468797/
https://www.ncbi.nlm.nih.gov/pubmed/26097520
http://dx.doi.org/10.1007/s12195-014-0364-5
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author Yan, Jie
Yao, Mingxi
Goult, Benjamin T.
Sheetz, Michael P.
author_facet Yan, Jie
Yao, Mingxi
Goult, Benjamin T.
Sheetz, Michael P.
author_sort Yan, Jie
collection PubMed
description A fundamental question in mechanobiology is how mechanical stimuli are sensed by mechanosensing proteins and converted into signals that direct cells to adapt to the external environment. A key function of cell adhesion to the extracellular matrix (ECM) is to transduce mechanical forces between cells and their extracellular environment. Talin, a cytoplasmic adapter essential for integrin-mediated adhesion to the ECM, links the actin cytoskeleton to integrin at the plasma membrane. Here, we review recent progress in the understanding of talin-dependent mechanosensing revealed by stretching single talin molecules. Rapid progress in single-molecule force manipulation technologies has made it possible to directly study the impact of mechanical force on talin’s conformations and its interactions with other signaling proteins. We also provide our views on how findings from such studies may bring new insights into understanding the principles of mechanobiology on a broader scale, and how such fundamental knowledge may be harnessed for mechanopharmacology.
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spelling pubmed-44687972015-06-17 Talin Dependent Mechanosensitivity of Cell Focal Adhesions Yan, Jie Yao, Mingxi Goult, Benjamin T. Sheetz, Michael P. Cell Mol Bioeng Article A fundamental question in mechanobiology is how mechanical stimuli are sensed by mechanosensing proteins and converted into signals that direct cells to adapt to the external environment. A key function of cell adhesion to the extracellular matrix (ECM) is to transduce mechanical forces between cells and their extracellular environment. Talin, a cytoplasmic adapter essential for integrin-mediated adhesion to the ECM, links the actin cytoskeleton to integrin at the plasma membrane. Here, we review recent progress in the understanding of talin-dependent mechanosensing revealed by stretching single talin molecules. Rapid progress in single-molecule force manipulation technologies has made it possible to directly study the impact of mechanical force on talin’s conformations and its interactions with other signaling proteins. We also provide our views on how findings from such studies may bring new insights into understanding the principles of mechanobiology on a broader scale, and how such fundamental knowledge may be harnessed for mechanopharmacology. Springer US 2014-11-04 2015 /pmc/articles/PMC4468797/ /pubmed/26097520 http://dx.doi.org/10.1007/s12195-014-0364-5 Text en © Biomedical Engineering Society 2014
spellingShingle Article
Yan, Jie
Yao, Mingxi
Goult, Benjamin T.
Sheetz, Michael P.
Talin Dependent Mechanosensitivity of Cell Focal Adhesions
title Talin Dependent Mechanosensitivity of Cell Focal Adhesions
title_full Talin Dependent Mechanosensitivity of Cell Focal Adhesions
title_fullStr Talin Dependent Mechanosensitivity of Cell Focal Adhesions
title_full_unstemmed Talin Dependent Mechanosensitivity of Cell Focal Adhesions
title_short Talin Dependent Mechanosensitivity of Cell Focal Adhesions
title_sort talin dependent mechanosensitivity of cell focal adhesions
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4468797/
https://www.ncbi.nlm.nih.gov/pubmed/26097520
http://dx.doi.org/10.1007/s12195-014-0364-5
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