Talin as a mechanosensitive signaling hub
Open accessAbstract
Cell adhesion to the extracellular matrix (ECM), mediated by transmembrane receptors of the integrin family, is exquisitely sensitive to biochemical, structural, and mechanical features of the ECM. Talin is a cytoplasmic protein consisting of a globular head domain and a series of α-helical bundles that form its long rod domain. Talin binds to the cytoplasmic domain of integrin β-subunits, activates integrins, couples them to the actin cytoskeleton, and regulates integrin signaling. Recent evidence suggests switch-like behavior of the helix bundles that make up the talin rod domains, where individual domains open at different tension levels, exerting positive or negative effects on different protein interactions. These results lead us to propose that talin functions as a mechanosensitive signaling hub that integrates multiple extracellular and intracellular inputs to define a major axis of adhesion signaling.
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Mechanical stretching unfolds talin and other mechanosensitive proteins, thus exposing cryptic binding sites.
“Mechanical stretching similarly unfolds talin and other mechanosensitive proteins, thus exposing cryptic binding sites [225, 226].”
From Intrinsically disordered proteins play diverse roles in cell signaling (2022) · cites this paper as [225]
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Direct observation of chaperone-modulated talin mechanics with single-molecule resolution
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Perception and response of skeleton to mechanical stress
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The focal adhesion protein talin is a mechanically gated A-kinase anchoring protein
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3D matrix adhesion feedback controls nuclear force coupling to drive invasive cell migration
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Self-citationWang, Q., Tian, X., Zhou, W., Wang, Y., Zhao, H., Li, J., Zhou, X., Zhang, H., Zhao, T., & Li, P. (2020) · Journal of Diabetes Research · doi:10.1155/2020/3634974 · Cited by 19 · see citing works
- Authors
- Goult, B. T., Yan, J., & Schwartz, M. A.
- Affiliations
- University of Kent (GB)
- National University of Singapore (SG)
- Wellcome Centre for Cell-Matrix Research (GB)
- Corresponding author
- Goult, Benjamin T.
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2018-09-25
- Volume
- 217
- Issue
- 11
- Pages
- 3776-3784
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC6219721
- OpenAlex
- W2894360011
- Cited by
- 250
- References
- 92
- Citations by year
- 2026: 27 · 2025: 28 · 2024: 38 · 2023: 24 · 2022: 38 · 2021: 37 · 2020: 28 · 2019: 29 · 2018: 1
- FWCI
- 3.44
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Kent Academic Repository (University of Kent) (acceptedVersion)
- Research Explorer (The University of Manchester) (acceptedVersion, other-oa)
- Funders
- Biotechnology and Biological Sciences Research Council (BB/N007336/1)
- National Research Foundation
- NRF (NRF-NRFI2016-03)
- Human Frontier Science Program (RGP00001/2016)
- Topics
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- talin, mechanosensitive signaling, integrin activation, cell adhesion, extracellular matrix, integrin beta subunit, actin cytoskeleton, adhesion signaling
- MeSH terms
- Protein Domains, Animals, Extracellular Matrix, Humans, Integrins, Talin, Protein Structure, Secondary, Mechanotransduction, Cellular
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