ArticleThe Biochemical journal2002
Further characterization of the interaction between the cytoskeletal proteins talin and vinculin.
Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 59 citations in OpenAlex.
- Mechanical regulation of talin through binding and history-dependent unfolding.Science advances · 2022Article
- Generic self-stabilization mechanism for biomolecular adhesions under load.Nature communications · 2022Article
- Article
- A distinct talin2 structure directs isoform specificity in cell adhesion.The Journal of biological chemistry · 2020Article
- Talin folding as the tuning fork of cellular mechanotransduction.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Phosphoinositides regulate force-independent interactions between talin, vinculin, and actin.eLife · 2020Article
- Direct observation of a coil-to-helix contraction triggered by vinculin binding to talin.Science advances · 2020Article
- Analysis of a vinculin homolog in a sponge (phylum Porifera) reveals that vertebrate-like cell adhesions emerged early in animal evolution.The Journal of biological chemistry · 2018Article
- Cell matrix adhesions in cancer: The proteins that form the glue.Oncotarget · 2017Review
- Drosophila vinculin is more harmful when hyperactive than absent, and can circumvent integrin to form adhesion complexes.Journal of cell science · 2016Article
- Binding of Vinculin to Lipid Membranes in Its Inhibited and Activated States.Biophysical journal · 2016Article
- Vinculin phosphorylation at residues Y100 and Y1065 is required for cellular force transmission.Journal of cell science · 2015Article
- Actomyosin-dependent formation of the mechanosensitive talin-vinculin complex reinforces actin anchoring.Nature communications · 2014Article
- Myosin II activity dependent and independent vinculin recruitment to the sites of E-cadherin-mediated cell-cell adhesion.BMC cell biology · 2011Article
- New insights into vinculin function and regulation.International review of cell and molecular biology · 2011Review
- A molecular dynamics investigation of vinculin activation.Biophysical journal · 2010Article
- Vinculin is a dually regulated actin filament barbed end-capping and side-binding protein.The Journal of biological chemistry · 2010Article
- Structural and biophysical properties of the integrin-associated cytoskeletal protein talin.Biophysical reviews · 2009Article
- Control of high affinity interactions in the talin C terminus: how talin domains coordinate protein dynamics in cell adhesions.The Journal of biological chemistry · 2009Article
- The talin rod IBS2 alpha-helix interacts with the beta3 integrin cytoplasmic tail membrane-proximal helix by establishing charge complementary salt bridges.The Journal of biological chemistry · 2008Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cytoskeletal protein talin, which is thought to couple integrins to F-actin, contains three binding sites (VBS1-VBS3) for vinculin, a protein implicated in the negative regulation of cell motility and whose activity is modulated by an intramolecular interaction between the vinculin head (Vh) and vinculin tail (Vt) domains. In the present study we show that recombinant talin polypeptides containing the three VBSs (VBS1, residues 498-636; VBS2, residues 727-965; and VBS3, residues 1943-2157) each bind tightly to the same or overlapping sites within vinculin(1-258). A short synthetic talin VBS3 peptide (residues 1944-1969) was sufficient to inhibit binding of a (125)I-labelled talin VBS3 polypeptide to vinculin(1-258), and NMR spectroscopy confirmed that this peptide forms a 1:1 complex in slow exchange with vinculin(1-258). Binding of the (125)I-labelled VBS3 polypeptide was markedly temperature dependent, but was not inhibited by 1 M salt or 10% (v/v) 2-methyl-2-propanol. Attempts to further define the talin-binding site within vinculin(1-258) using a gel-blot assay were unsuccessful, but near maximal talin-binding activity was retained by a construct spanning vinculin residues 1-131 in a yeast two-hybrid assay. Interestingly, the talin VBS3 polypeptide was a potent inhibitor of the Vh-Vt interaction, and the VBS3 synthetic peptide was able to expose the actin-binding site in intact vinculin, which is otherwise masked by the Vh-Vt interaction. The results suggest that under certain conditions, talin may be an effective activator of vinculin.
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