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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...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Company of Biologists Ltd
2021
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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. |
format | Online Article Text |
id | pubmed-8697387 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | The Company of Biologists Ltd |
record_format | MEDLINE/PubMed |
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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