ArticleStructure (London, England : 1993)2010
The structure of the talin/integrin complex at a lipid bilayer: an NMR and MD simulation study.
Article in Structure (London, England : 1993), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
41 citing papers in PubMed.
- De novo talin-1 variant L353F connects multifaceted clinical symptoms to alterations in talin-1 function.The Biochemical journal · 2025Article
- Talin variant P229S compromises integrin activation and associates with multifaceted clinical symptoms.Human molecular genetics · 2022Article
- Review
- Insight Into Pathological Integrin αIIbβ3 Activation From Safeguarding The Inactive State.Journal of molecular biology · 2021Article
- Kindlin Assists Talin to Promote Integrin Activation.Biophysical journal · 2020Article
- 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
- Interactions of the EphA2 Kinase Domain with PIPs in Membranes: Implications for Receptor Function.Structure (London, England : 1993) · 2018Article
- The Integrin Receptor in Biologically Relevant Bilayers: Insights from Molecular Dynamics Simulations.The Journal of membrane biology · 2017Article
- Phosphatidylinositol 4,5-Bisphosphate Modulates the Affinity of Talin-1 for Phospholipid Bilayers and Activates Its Autoinhibited Form.Biochemistry · 2016Article
- A Conserved Ectodomain-Transmembrane Domain Linker Motif Tunes the Allosteric Regulation of Cell Surface Receptors.The Journal of biological chemistry · 2016Article
- Conformational equilibrium of talin is regulated by anionic lipids.Biochimica et biophysica acta · 2016Article
- Multiscale Simulations Suggest a Mechanism for the Association of the Dok7 PH Domain with PIP-Containing Membranes.PLoS computational biology · 2016Article
- Atomic-level description of protein-lipid interactions using an accelerated membrane model.Biochimica et biophysica acta · 2016Review
- Structures of the EphA2 Receptor at the Membrane: Role of Lipid Interactions.Structure (London, England : 1993) · 2016Article
- NMR Characterization and Membrane Interactions of the Loop Region of Kindlin-3 F1 Subdomain.PloS one · 2016Article
- Anomalous Dynamics of a Lipid Recognition Protein on a Membrane Surface.Scientific reports · 2015Article
- PIP kinases define PI4,5P₂signaling specificity by association with effectors.Biochimica et biophysica acta · 2015Review
- Membrane Association of the Diphtheria Toxin Translocation Domain Studied by Coarse-Grained Simulations and Experiment.The Journal of membrane biology · 2015Article
- Efficient Exploration of Membrane-Associated Phenomena at Atomic Resolution.The Journal of membrane biology · 2015Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Integrins are cell surface receptors crucial for cell migration and adhesion. They are activated by interactions of the talin head domain with the membrane surface and the integrin β cytoplasmic tail. Here, we use coarse-grained molecular dynamic simulations and nuclear magnetic resonance spectroscopy to elucidate the membrane-binding surfaces of the talin head (F2-F3) domain. In particular, we show that mutations in the four basic residues (K258E, K274E, R276E, and K280E) in the F2 binding surface reduce the affinity of the F2-F3 for the membrane and modify its orientation relative to the bilayer. Our results highlight the key role of anionic lipids in talin/membrane interactions. Simulation of the F2-F3 in complex with the α/β transmembrane dimer reveals information for its orientation relative to the membrane. Our studies suggest that the perturbed orientation of talin relative to the membrane in the F2 mutant would be expected to in turn perturb talin/integrin interactions.
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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.