ArticleProtein science : a publication of the Protein Society2012
Crystal structure of vinculin in complex with vinculin binding site 50 (VBS50), the integrin binding site 2 (IBS2) of talin.
Article in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 13 citations in OpenAlex.
- Environmental Toxicants and Their Disruption of Integrin Signaling in Lipid Rafts.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- A distinct talin2 structure directs isoform specificity in cell adhesion.The Journal of biological chemistry · 2020Article
- The interaction of talin with the cell membrane is essential for integrin activation and focal adhesion formation.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Differential lipid binding of vinculin isoforms promotes quasi-equivalent dimerization.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Spider Silk Peptide Is a Compact, Linear Nanospring Ideal for Intracellular Tension Sensing.Nano letters · 2016Article
- The metavinculin tail domain directs constitutive interactions with raver1 and vinculin RNA.Journal of molecular biology · 2012Article
- The cytoskeletal protein α-catenin unfurls upon binding to vinculin.The Journal of biological chemistry · 2012Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cytoskeletal protein talin activates integrin receptors by binding of its FERM domain to the cytoplasmic tail of β-integrin. Talin also couples integrins to the actin cytoskeleton, largely by binding to and activating the cytoskeletal protein vinculin, which binds to F-actin through the agency of its five-helix bundle tail (Vt) domain. Talin activates vinculin by means of buried amphipathic α-helices coined vinculin binding sites (VBSs) that reside within numerous four- and five-helix bundle domains that comprise the central talin rod, which are released from their buried locales by means of mechanical tension on the integrin:talin complex. In turn, these VBSs bind to the N-terminal seven-helix bundle (Vh1) domain of vinculin, creating an entirely new helix bundle that severs its head-tail interactions. Interestingly, talin harbors a second integrin binding site coined IBS2 that consists of two five-helix bundle domains that also contain a VBS (VBS50). Here we report the crystal structure of VBS50 in complex with vinculin at 2.3 Å resolution and show that intramolecular interactions of VBS50 within IBS2 are much more extensive versus its interactions with vinculin. Indeed, the IBS2-vinculin interaction only occurs at physiological temperature and the affinity of VBS50 for vinculin is about 30 times less than other VBSs. The data support a model where integrin binding destabilizes IBS2 to allow it to bind to vinculin.
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