ArticlePLoS computational biology2013
Conformational changes in talin on binding to anionic phospholipid membranes facilitate signaling by integrin transmembrane helices.
Article in PLoS computational biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 33 citations in OpenAlex.
- Advances in modeling cellular mechanical perceptions and responses via the membrane-cytoskeleton-nucleus machinery.Mechanobiology in medicine · 2024Review
- Molecular dynamics simulations reveal membrane lipid interactions of the full-length lymphocyte specific kinase (Lck).Scientific reports · 2022Article
- Mechanistic Understanding from Molecular Dynamics in Pharmaceutical Research 2: Lipid Membrane in Drug Design.Pharmaceuticals (Basel, Switzerland) · 2021Review
- Multi-scale simulations of the T cell receptor reveal its lipid interactions, dynamics and the arrangement of its cytoplasmic region.PLoS computational biology · 2021Article
- The F1 loop of the talin head domain acts as a gatekeeper in integrin activation and clustering.Journal of cell science · 2020Article
- Kindlin Assists Talin to Promote Integrin Activation.Biophysical journal · 2020Article
- Filopodia and focal adhesions: An integrated system driving branching morphogenesis in neuronal pathfinding and angiogenesis.Developmental biology · 2019Review
- Self-Assembly of Polymer-Encased Lipid Nanodiscs and Membrane Protein Reconstitution.The journal of physical chemistry. B · 2019Article
- Emerging Diversity in Lipid-Protein Interactions.Chemical reviews · 2019Review
- Characterization of Lipid-Protein Interactions and Lipid-Mediated Modulation of Membrane Protein Function through Molecular Simulation.Chemical reviews · 2019Review
- Identification of AtHsp90.6 involved in early embryogenesis and its structure prediction by molecular dynamics simulations.Royal Society open science · 2019Article
- The membrane-distal regions of integrin α cytoplasmic domains contribute differently to integrin inside-out activation.Scientific reports · 2018Article
- The Integrin Receptor in Biologically Relevant Bilayers: Insights from Molecular Dynamics Simulations.The Journal of membrane biology · 2017Article
- Computational and theoretical approaches for studies of a lipid recognition protein on biological membranes.Biophysics and physicobiology · 2017Review
- Conformational equilibrium of talin is regulated by anionic lipids.Biochimica et biophysica acta · 2016Article
- Efficient Exploration of Membrane-Associated Phenomena at Atomic Resolution.The Journal of membrane biology · 2015Review
- PIP kinases define PI4,5P₂signaling specificity by association with effectors.Biochimica et biophysica acta · 2015Review
- The dual structural roles of the membrane distal region of the α-integrin cytoplasmic tail during integrin inside-out activation.Journal of cell science · 2015Article
- Article
- The talin head domain reinforces integrin-mediated adhesion by promoting adhesion complex stability and clustering.PLoS genetics · 2014Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Integrins are heterodimeric (αβ) cell surface receptors that are activated to a high affinity state by the formation of a complex involving the α/β integrin transmembrane helix dimer, the head domain of talin (a cytoplasmic protein that links integrins to actin), and the membrane. The talin head domain contains four sub-domains (F0, F1, F2 and F3) with a long cationic loop inserted in the F1 domain. Here, we model the binding and interactions of the complete talin head domain with a phospholipid bilayer, using multiscale molecular dynamics simulations. The role of the inserted F1 loop, which is missing from the crystal structure of the talin head, PDB:3IVF, is explored. The results show that the talin head domain binds to the membrane predominantly via cationic regions on the F2 and F3 subdomains and the F1 loop. Upon binding, the intact talin head adopts a novel V-shaped conformation which optimizes its interactions with the membrane. Simulations of the complex of talin with the integrin α/β TM helix dimer in a membrane, show how this complex promotes a rearrangement, and eventual dissociation of, the integrin α and β transmembrane helices. A model for the talin-mediated integrin activation is proposed which describes how the mutual interplay of interactions between transmembrane helices, the cytoplasmic talin protein, and the lipid bilayer promotes integrin inside-out activation.
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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.