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Talin in mechanotransduction and mechanomemory at a glance

Talins are cytoskeletal linker proteins that consist of an N-terminal head domain, a flexible neck region and a C-terminal rod domain made of 13 helical bundles. The head domain binds integrin β-subunit cytoplasmic tails, which triggers integrin conformational activation to increase affinity for ext...

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Autores principales: Goult, Benjamin T., Brown, Nicholas H., Schwartz, Martin A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Company of Biologists Ltd 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8697387/
https://www.ncbi.nlm.nih.gov/pubmed/34708856
http://dx.doi.org/10.1242/jcs.258749
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author Goult, Benjamin T.
Brown, Nicholas H.
Schwartz, Martin A.
author_facet Goult, Benjamin T.
Brown, Nicholas H.
Schwartz, Martin A.
author_sort Goult, Benjamin T.
collection PubMed
description Talins are cytoskeletal linker proteins that consist of an N-terminal head domain, a flexible neck region and a C-terminal rod domain made of 13 helical bundles. The head domain binds integrin β-subunit cytoplasmic tails, which triggers integrin conformational activation to increase affinity for extracellular matrix proteins. The rod domain links to actin filaments inside the cell to transmit mechanical loads and serves as a mechanosensitive signalling hub for the recruitment of many other proteins. The α-helical bundles function as force-dependent switches – proteins that interact with folded bundles are displaced when force induces unfolding, exposing previously cryptic binding sites for other ligands. This leads to the notion of a talin code. In this Cell Science at a Glance article and the accompanying poster, we propose that the multiple switches within the talin rod function to process and store time- and force-dependent mechanical and chemical information.
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spelling pubmed-86973872022-01-07 Talin in mechanotransduction and mechanomemory at a glance Goult, Benjamin T. Brown, Nicholas H. Schwartz, Martin A. J Cell Sci Cell Science at A Glance Talins are cytoskeletal linker proteins that consist of an N-terminal head domain, a flexible neck region and a C-terminal rod domain made of 13 helical bundles. The head domain binds integrin β-subunit cytoplasmic tails, which triggers integrin conformational activation to increase affinity for extracellular matrix proteins. The rod domain links to actin filaments inside the cell to transmit mechanical loads and serves as a mechanosensitive signalling hub for the recruitment of many other proteins. The α-helical bundles function as force-dependent switches – proteins that interact with folded bundles are displaced when force induces unfolding, exposing previously cryptic binding sites for other ligands. This leads to the notion of a talin code. In this Cell Science at a Glance article and the accompanying poster, we propose that the multiple switches within the talin rod function to process and store time- and force-dependent mechanical and chemical information. The Company of Biologists Ltd 2021-10-28 /pmc/articles/PMC8697387/ /pubmed/34708856 http://dx.doi.org/10.1242/jcs.258749 Text en © 2021. Published by The Company of Biologists Ltd https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed.
spellingShingle Cell Science at A Glance
Goult, Benjamin T.
Brown, Nicholas H.
Schwartz, Martin A.
Talin in mechanotransduction and mechanomemory at a glance
title Talin in mechanotransduction and mechanomemory at a glance
title_full Talin in mechanotransduction and mechanomemory at a glance
title_fullStr Talin in mechanotransduction and mechanomemory at a glance
title_full_unstemmed Talin in mechanotransduction and mechanomemory at a glance
title_short Talin in mechanotransduction and mechanomemory at a glance
title_sort talin in mechanotransduction and mechanomemory at a glance
topic Cell Science at A Glance
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8697387/
https://www.ncbi.nlm.nih.gov/pubmed/34708856
http://dx.doi.org/10.1242/jcs.258749
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