ArticleBiophysical reviews2009
Structural and biophysical properties of the integrin-associated cytoskeletal protein talin.
Article in Biophysical reviews, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 65 citations in OpenAlex.
- Inside-out integrin activation is essential for early mammalian development.Molecular biology of the cell · 2025Article
- Biochemical and structural bases for talin ABSs-F-actin interactions.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Calpain Promotes LPS-induced Lung Endothelial Barrier Dysfunction via Cleavage of Talin.American journal of respiratory cell and molecular biology · 2023Article
- A molecular optomechanics approach reveals functional relevance of force transduction across talin and desmoplakin.Science advances · 2023Article
- Vinculin Y822 is an important determinant of ligand binding.Journal of cell science · 2023Article
- The structural basis of β2 integrin intra-cellular multi-protein complexes.Biophysical reviews · 2022Review
- Integrin Regulators in Neutrophils.Cells · 2022Review
- Fibrinogen Mitigates Prion-Mediated Platelet Activation and Neuronal Cell Toxicity.Frontiers in cell and developmental biology · 2022Article
- Prognostic value of Talin-1 in renal cell carcinoma and its association with B7-H3.Cancer biomarkers : section A of Disease markers · 2022Article
- 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
- Article
- The F1 loop of the talin head domain acts as a gatekeeper in integrin activation and clustering.Journal of cell science · 2020Article
- Basic Fibroblast Growth Factor 2-Induced Proteome Changes Endorse Lewy Body Pathology in Hippocampal Neurons.iScience · 2020Article
- The Role of Hypoxia in Corneal Extracellular Matrix Deposition and Cell Motility.Anatomical record (Hoboken, N.J. : 2007) · 2020Article
- Talin and Kindlin as Integrin-Activating Proteins: Focus on the Heart.Pediatric cardiology · 2019Review
- Rare Missense Variants in TLN1 Are Associated With Familial and Sporadic Spontaneous Coronary Artery Dissection.Circulation. Genomic and precision medicine · 2019Article
- The extracellular matrix-myosin pathway in mechanotransduction: from molecule to tissue.Emerging topics in life sciences · 2018Article
- Mechanical unfolding reveals stable 3-helix intermediates in talin and α-catenin.PLoS computational biology · 2018Article
- Phosphatidylinositol 4,5-Bisphosphate Modulates the Affinity of Talin-1 for Phospholipid Bilayers and Activates Its Autoinhibited Form.Biochemistry · 2016Article
- Emergence and subsequent functional specialization of kindlins during evolution of cell adhesiveness.Molecular biology of the cell · 2015Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Talin is a large cytoskeletal protein (2541 amino acid residues) which plays a key role in integrin-mediated events that are crucial for cell adhesion, migration, proliferation and survival. This review summarises recent work on the structure of talin and on some of the structurally better defined interactions with other proteins. The N-terminal talin head (approx. 50 kDa) consists of an atypical FERM domain linked to a long flexible rod (approx. 220 kDa) made up of a series of amphipathic helical bundle domains. The F3 FERM subdomain in the head binds the cytoplasmic tail of integrins, but this interaction can be inhibited by an interaction of F3 with a helical bundle in the talin rod, the so-called "autoinhibited form" of the molecule. The talin rod contains a second integrin-binding site, at least two actin-binding sites and a large number of binding sites for vinculin, which is important in reinforcing the initial integrin-actin link mediated by talin. The vinculin binding sites are defined by hydrophobic residues buried within helical bundles, and these must unfold to allow vinculin binding. Recent experiments suggest that this unfolding may be mediated by mechanical force exerted on the talin molecule by actomyosin contraction. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s12551-009-0009-4) contains supplementary material, which is available to authorized users.
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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.