ArticleJournal of the Royal Society, Interface2014
Actin flow and talin dynamics govern rigidity sensing in actin-integrin linkage through talin extension.
Article in Journal of the Royal Society, Interface, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- Cancer cell response to extrinsic and intrinsic mechanical cue: opportunities for tumor apoptosis strategies.Regenerative biomaterials · 2024Review
- Biomechanical, biophysical and biochemical modulators of cytoskeletal remodelling and emergent stem cell lineage commitment.Communications biology · 2023Review
- Mechanoregulation and pathology of YAP/TAZ via Hippo and non-Hippo mechanisms.Clinical and translational medicine · 2018Review
- Proteomic changes of CD4Experimental and therapeutic medicine · 2017Article
- Distinct focal adhesion protein modules control different aspects of mechanotransduction.Journal of cell science · 2017Article
- Matrix metalloproteinase-9-dependent mechanisms of reduced contractility and increased stiffness in the aging heart.Proteomics. Clinical applications · 2016Article
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
At cell-substrate adhesion sites, the linkage between actin filaments and integrin is regulated by mechanical stiffness of the substrate. Of potential molecular regulators, the linker proteins talin and vinculin are of particular interest because mechanical extension of talin induces vinculin binding with talin, which reinforces the actin-integrin linkage. For understanding the molecular and biophysical mechanism of rigidity sensing at cell-substrate adhesion sites, we constructed a simple physical model to examine a role of talin extension in the stiffness-dependent regulation of actin-integrin linkage. We show that talin molecules linking between retrograding actin filaments and substrate-bound integrin are extended in a manner dependent on substrate stiffness. The model predicts that, in adhesion complexes containing ≈30 talin links, talin is extended enough for vinculin binding when the substrate is stiffer than 1 kPa. The lifetime of talin links needs to be 2-5 s to achieve an appropriate response of talin extension against substrate stiffness. Furthermore, changes in actin velocity drastically shift the range of substrate stiffness that induces talin-vinculin binding. Our results suggest that talin extension is a key step in sensing and responding to substrate stiffness at cell adhesion sites.
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Registered trials
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