ArticleBiophysical journal2014
The talin dimer structure orientation is mechanically regulated.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 25 citations in OpenAlex.
- The actin binding sites of talin have both distinct and complementary roles in cell-ECM adhesion.PLoS genetics · 2024Article
- Recent Advances and Prospects in the Research of Nascent Adhesions.Frontiers in physiology · 2020Review
- Integrin nanoclusters can bridge thin matrix fibres to form cell-matrix adhesions.Nature materials · 2019Article
- Building nanobridges for cell adhesion.Nature materials · 2019Article
- Kindlin Is Mechanosensitive: Force-Induced Conformational Switch Mediates Cross-Talk among Integrins.Biophysical journal · 2019Article
- Pulmonary Endothelial Mechanical Sensing and Signaling, a Story of Focal Adhesions and Integrins in Ventilator Induced Lung Injury.Frontiers in physiology · 2019Review
- Mechanical unfolding reveals stable 3-helix intermediates in talin and α-catenin.PLoS computational biology · 2018Article
- Conformational states during vinculin unlocking differentially regulate focal adhesion properties.Scientific reports · 2018Article
- Cellular Mechanotransduction: From Tension to Function.Frontiers in physiology · 2018Review
- Tissue Force Programs Cell Fate and Tumor Aggression.Cancer discovery · 2017Review
- Mechanosensitive Conformation of Vinculin Regulates Its Binding to MAPK1.Biophysical journal · 2017Article
- The PET and LIM1-2 domains of testin contribute to intramolecular and homodimeric interactions.PloS one · 2017Article
- All Subdomains of the Talin Rod Are Mechanically Vulnerable and May Contribute To Cellular Mechanosensing.ACS nano · 2016Article
- Cooperative Vinculin Binding to Talin Mapped by Time-Resolved Super Resolution Microscopy.Nano letters · 2016Article
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Authors and funding
2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Formation of a stable cell-substrate contact can be regulated by mechanical force, especially at the focal adhesion. Individual proteins that make up the focal adhesions, such as talin, can exhibit mechanosensing. We previously described one mode of talin mechanosensing in which the vinculin-binding site of talin is exposed after force-induced stretch of a single talin rod domain. Here, we describe a second mode of talin mechanosensing in which the talin dimer itself can adopt different orientations in response to mechanical stimulation. Using molecular dynamics models, we demonstrate that the C-terminus region of the talin dimer is flexible mainly at the linker between the dimerization helices and the nearby actin-binding helical bundle. Our molecular dynamics simulations reveal two possible orientations of the talin dimer at its C-terminus. The extracellular matrix (ECM)-bound integrins cross-linked by talin can be forced apart leading to an elongated orientation of the talin dimer, and the ECM-bound integrins can be forced together by the ECM producing a collapsed orientation of the talin dimer. Formation of the elongated orientation is shown to be more favorable. Switching between the two talin dimer orientations constitutes a mode of mechanosensing.
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