ArticleThe Journal of biological chemistry2020
A distinct talin2 structure directs isoform specificity in cell adhesion.
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 17 citations in OpenAlex.
- Mechanical Load-Induced Upregulation of Talin2 through Non-Canonical Deubiquitination of OTUB1 Drives Facet Joint Osteoarthritis Pathogenesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Molecular basis of β2 integrin activation by talin unveils subunit-specific mechanisms of integrin signaling.Cell reports · 2025Article
- Environmental Toxicants and Their Disruption of Integrin Signaling in Lipid Rafts.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- High-resolution snapshots of the talin auto-inhibitory states suggest roles in cell adhesion and signaling.Nature communications · 2024Article
- Membrane-induced 2D phase separation of the focal adhesion protein talin.Nature communications · 2024Article
- Epigenome-wide association study identifies novel genes associated with ischemic stroke.Clinical epigenetics · 2023Article
- Plakophilin-3 Binds the Membrane and Filamentous Actin without Bundling F-Actin.International journal of molecular sciences · 2023Article
- Review
- Initiation of focal adhesion assembly by talin and kindlin: A dynamic view.Protein science : a publication of the Protein Society · 2021Review
- Crystal structure of the FERM-folded talin head reveals the determinants for integrin binding.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The F1 loop of the talin head domain acts as a gatekeeper in integrin activation and clustering.Journal of cell science · 2020Article
- Optogenetics-based localization of talin to the plasma membrane promotes activation of β3 integrins.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Integrin receptors regulate normal cellular processes such as signaling, cell migration, adhesion to the extracellular matrix, and leukocyte function. Talin recruitment to the membrane is necessary for its binding to and activation of integrin. Vertebrates have two highly conserved talin homologs that differ in their expression patterns. The F1-F3 FERM subdomains of cytoskeletal proteins resemble a cloverleaf, but in talin1, its F1 subdomain and additional F0 subdomain align more linearly with its F2 and F3 subdomains. Here, we present the talin2 crystal structure, revealing that its F0-F1 di-subdomain displays another unprecedented constellation, whereby the F0-F1-F2 adopts a new cloverleaf-like arrangement. Using multiangle light scattering (MALS), fluorescence lifetime imaging (FLIM), and FRET analyses, we found that substituting the corresponding residues in talin2 that abolish lipid binding in talin1 disrupt the binding of talin to the membrane, focal adhesion formation, and cell spreading. Our results provide the molecular details of the functions of specific talin isoforms in cell adhesion.
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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.