ArticleNature communications2020
Talin dissociates from RIAM and associates to vinculin sequentially in response to the actomyosin force.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 41 citations in OpenAlex.
- The Degeneration Paradox: Severely Degenerated Cervical Nucleus Pulposus Cells Display Enhanced Mechanoplasticity Under Moderate Cyclic Tensile Strain.Biomolecules · 2026Article
- Actomyosin-dependent assembly of the mechanosensitive machinery from adherens junctions triggers actin polymerization and organization.Science advances · 2026Article
- Development of three-colour FRET cascade for force sensing of the putative RIAM-vinculin interaction in fibroblasts.Communications chemistry · 2025Article
- Force writes memory: proline isomerization as a molecular memory switch.Biochemical Society transactions · 2025Review
- Reconstituted systems for studying the architecture and dynamics of actin networks.The Biochemical journal · 2025Review
- Vinculin-Arp2/3 interaction inhibits branched actin assembly to control migration and proliferation.Life science alliance · 2025Article
- TLN1: an oncogene associated with tumorigenesis and progression.Discover oncology · 2024Review
- Talin and vinculin combine their activities to trigger actin assembly.Nature communications · 2024Article
- Caskin2 is a novel talin- and Abi1-binding protein that promotes cell motility.Journal of cell science · 2024Article
- Organization, dynamics and mechanoregulation of integrin-mediated cell-ECM adhesions.Nature reviews. Molecular cell biology · 2023Review
- The mechanical cell - the role of force dependencies in synchronising protein interaction networks.Journal of cell science · 2022Review
- Review
- Talin‑1 interaction network in cellular mechanotransduction (Review).International journal of molecular medicine · 2022Review
- Structural, biochemical, and functional properties of the Rap1-Interacting Adaptor Molecule (RIAM).Biomedical journal · 2022Review
- The MeshCODE to scale-visualising synaptic binary information.Frontiers in cellular neuroscience · 2022Article
- Expression of the phagocytic receptors αFrontiers in immunology · 2022Article
- Viscoelasticity, Like Forces, Plays a Role in Mechanotransduction.Frontiers in cell and developmental biology · 2022Review
- Talin in mechanotransduction and mechanomemory at a glance.Journal of cell science · 2021Article
- LIM domain proteins in cell mechanobiology.Cytoskeleton (Hoboken, N.J.) · 2021Review
- Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cells reinforce adhesion strength and cytoskeleton anchoring in response to the actomyosin force. The mechanical stretching of talin, which exposes cryptic vinculin-binding sites, triggers this process. The binding of RIAM to talin could regulate this mechanism. However, the mechanosensitivity of the talin-RIAM complex has never been tested. It is also not known whether RIAM controls the mechanosensitivity of the talin-vinculin complex. To address these issues, we designed an in vitro microscopy assay with purified proteins in which the actomyosin force controls RIAM and vinculin-binding to talin. We demonstrate that actomyosin triggers RIAM dissociation from several talin domains. Actomyosin also provokes the sequential exchange of RIAM for vinculin on talin. The effect of RIAM on this force-dependent binding of vinculin to talin varies from one talin domain to another. This mechanism could allow talin to biochemically code a wide range of forces by selecting different combinations of partners.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.