ArticleThe Journal of biological chemistry2010
Central region of talin has a unique fold that binds vinculin and actin.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 76 citations in OpenAlex.
- Conformational flexibility of talin enables force-free sampling of activation-competent states.Communications chemistry · 2026Article
- Force writes memory: proline isomerization as a molecular memory switch.Biochemical Society transactions · 2025Review
- The Life of a Kidney Podocyte.Acta physiologica (Oxford, England) · 2025Review
- TLNRD1 is a CCM complex component and regulates endothelial barrier integrity.The Journal of cell biology · 2024Article
- Mechanically operated signalling scaffolds.Biochemical Society transactions · 2024Review
- The actin binding sites of talin have both distinct and complementary roles in cell-ECM adhesion.PLoS genetics · 2024Article
- Article
- Calpain Promotes LPS-induced Lung Endothelial Barrier Dysfunction via Cleavage of Talin.American journal of respiratory cell and molecular biology · 2023Article
- Inhibition of talin-induced integrin activation by a double-hit stapled peptide.Structure (London, England : 1993) · 2023Article
- The structural basis of the talin-KANK1 interaction that coordinates the actin and microtubule cytoskeletons at focal adhesions.Open biology · 2023Article
- Mechanical regulation of talin through binding and history-dependent unfolding.Science advances · 2022Article
- The MeshCODE to scale-visualising synaptic binary information.Frontiers in cellular neuroscience · 2022Article
- Talin rod domain-containing protein 1 (TLNRD1) is a novel actin-bundling protein which promotes filopodia formation.The Journal of cell biology · 2021Article
- Talin mechanosensitivity is modulated by a direct interaction with cyclin-dependent kinase-1.The Journal of biological chemistry · 2021Article
- Article
- Talin-dependent integrin activation is required for endothelial proliferation and postnatal angiogenesis.Angiogenesis · 2021Article
- Cancer associated talin point mutations disorganise cell adhesion and migration.Scientific reports · 2021Article
- Alterations of Growth and Focal Adhesion Molecules in Human Breast Cancer Cells Exposed to the Random Positioning Machine.Frontiers in cell and developmental biology · 2021Article
- A distinct talin2 structure directs isoform specificity in cell adhesion.The Journal of biological chemistry · 2020Article
- Morphological and Molecular Changes in Juvenile Normal Human Fibroblasts Exposed to Simulated Microgravity.Scientific reports · 2019Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Talin is an adaptor protein that couples integrins to F-actin. Structural studies show that the N-terminal talin head contains an atypical FERM domain, whereas the N- and C-terminal parts of the talin rod include a series of α-helical bundles. However, determining the structure of the central part of the rod has proved problematic. Residues 1359-1659 are homologous to the MESDc1 gene product, and we therefore expressed this region of talin in Escherichia coli. The crystal structure shows a unique fold comprised of a 5- and 4-helix bundle. The 5-helix bundle is composed of nonsequential helices due to insertion of the 4-helix bundle into the loop at the C terminus of helix α3. The linker connecting the bundles forms a two-stranded anti-parallel β-sheet likely limiting the relative movement of the two bundles. Because the 5-helix bundle contains the N and C termini of this module, we propose that it is linked by short loops to adjacent bundles, whereas the 4-helix bundle protrudes from the rod. This suggests the 4-helix bundle has a unique role, and its pI (7.8) is higher than other rod domains. Both helical bundles contain vinculin-binding sites but that in the isolated 5-helix bundle is cryptic, whereas that in the isolated 4-helix bundle is constitutively active. In contrast, both bundles are required for actin binding. Finally, we show that the MESDc1 protein, which is predicted to have a similar fold, is a novel actin-binding protein.
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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.