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Talin-1 interaction network in cellular mechanotransduction (Review)
The mechanical signals within the extracellular matrix (ECM) regulate cell growth, proliferation and differentiation, and integrins function as the hub between the ECM and cellular actin. Focal adhesions (FAs) are multi-protein, integrin-containing complexes, acting as tension-sensing anchoring poin...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
D.A. Spandidos
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8930095/ https://www.ncbi.nlm.nih.gov/pubmed/35266014 http://dx.doi.org/10.3892/ijmm.2022.5116 |
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author | Zhao, Ye Lykov, Nikita Tzeng, Chimeng |
author_facet | Zhao, Ye Lykov, Nikita Tzeng, Chimeng |
author_sort | Zhao, Ye |
collection | PubMed |
description | The mechanical signals within the extracellular matrix (ECM) regulate cell growth, proliferation and differentiation, and integrins function as the hub between the ECM and cellular actin. Focal adhesions (FAs) are multi-protein, integrin-containing complexes, acting as tension-sensing anchoring points that bond cells to the extracellular microenvironment. Talin-1 serves as the central protein of FAs that participates in the activation of integrins and connects them with the actin cytoskeleton. As a cytoplasmic protein, Talin-1 consists of a globular head domain and a long rod comprised of a series of α-helical bundles. The unique structure of the Talin-1 rod domain permits folding and unfolding in response to the mechanical stress, revealing various binding sites. Thus, conformation changes of the Talin-1 rod domain enable the cell to convert mechanical signals into chemical through multiple signaling pathways. The present review discusses the binding partners of Talin-1, their interactions, effects on the cellular processes, and their possible roles in diseases. |
format | Online Article Text |
id | pubmed-8930095 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | D.A. Spandidos |
record_format | MEDLINE/PubMed |
spelling | pubmed-89300952022-03-25 Talin-1 interaction network in cellular mechanotransduction (Review) Zhao, Ye Lykov, Nikita Tzeng, Chimeng Int J Mol Med Articles The mechanical signals within the extracellular matrix (ECM) regulate cell growth, proliferation and differentiation, and integrins function as the hub between the ECM and cellular actin. Focal adhesions (FAs) are multi-protein, integrin-containing complexes, acting as tension-sensing anchoring points that bond cells to the extracellular microenvironment. Talin-1 serves as the central protein of FAs that participates in the activation of integrins and connects them with the actin cytoskeleton. As a cytoplasmic protein, Talin-1 consists of a globular head domain and a long rod comprised of a series of α-helical bundles. The unique structure of the Talin-1 rod domain permits folding and unfolding in response to the mechanical stress, revealing various binding sites. Thus, conformation changes of the Talin-1 rod domain enable the cell to convert mechanical signals into chemical through multiple signaling pathways. The present review discusses the binding partners of Talin-1, their interactions, effects on the cellular processes, and their possible roles in diseases. D.A. Spandidos 2022-05 2022-03-09 /pmc/articles/PMC8930095/ /pubmed/35266014 http://dx.doi.org/10.3892/ijmm.2022.5116 Text en Copyright: © Zhao et al. https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License (https://creativecommons.org/licenses/by-nc-nd/4.0/) , which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made. |
spellingShingle | Articles Zhao, Ye Lykov, Nikita Tzeng, Chimeng Talin-1 interaction network in cellular mechanotransduction (Review) |
title | Talin-1 interaction network in cellular mechanotransduction (Review) |
title_full | Talin-1 interaction network in cellular mechanotransduction (Review) |
title_fullStr | Talin-1 interaction network in cellular mechanotransduction (Review) |
title_full_unstemmed | Talin-1 interaction network in cellular mechanotransduction (Review) |
title_short | Talin-1 interaction network in cellular mechanotransduction (Review) |
title_sort | talin-1 interaction network in cellular mechanotransduction (review) |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8930095/ https://www.ncbi.nlm.nih.gov/pubmed/35266014 http://dx.doi.org/10.3892/ijmm.2022.5116 |
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