ArticleProceedings of the National Academy of Sciences of the United States of America2011
Multiscale simulations suggest a mechanism for integrin inside-out activation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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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
35 citing papers in PubMed, 65 citations in OpenAlex.
- A computational study for understanding the impact of p120-catenin on the cis-dimerization of cadherin.Journal of molecular cell biology · 2024Article
- Multiscale models of integrins and cellular adhesions.Current opinion in structural biology · 2023Review
- Assessing a computational pipeline to identify binding motifs to theFrontiers in chemistry · 2023Article
- Roles of Membrane Domains in Integrin-Mediated Cell Adhesion.International journal of molecular sciences · 2020Review
- Multiscale model of integrin adhesion assembly.PLoS computational biology · 2019Article
- Self-Assembly of Polymer-Encased Lipid Nanodiscs and Membrane Protein Reconstitution.The journal of physical chemistry. B · 2019Article
- Characterization of Lipid-Protein Interactions and Lipid-Mediated Modulation of Membrane Protein Function through Molecular Simulation.Chemical reviews · 2019Review
- Emerging Diversity in Lipid-Protein Interactions.Chemical reviews · 2019Review
- Coarse-Grained Simulation of Full-Length Integrin Activation.Biophysical journal · 2019Article
- On the contributing role of the transmembrane domain for subunit-specific sensitivity of integrin activation.Scientific reports · 2018Article
- Transmission of integrin β7 transmembrane domain topology enables gut lymphoid tissue development.The Journal of cell biology · 2018Article
- Changes in Cholesterol Level Alter Integrin Sequestration in Raft-Mimicking Lipid Mixtures.Biophysical journal · 2018Article
- The Integrin Receptor in Biologically Relevant Bilayers: Insights from Molecular Dynamics Simulations.The Journal of membrane biology · 2017Article
- Epigallocatechin gallate has pleiotropic effects on transmembrane signaling by altering the embedding of transmembrane domains.The Journal of biological chemistry · 2017Article
- Structural heterogeneity of the μ-opioid receptor's conformational ensemble in the apo state.Scientific reports · 2017Article
- Conformational equilibrium of talin is regulated by anionic lipids.Biochimica et biophysica acta · 2016Article
- Review
- Atomic-level description of protein-lipid interactions using an accelerated membrane model.Biochimica et biophysica acta · 2016Review
- Key diffusion mechanisms involved in regulating bidirectional water permeation across E. coli outer membrane lectin.Scientific reports · 2016Article
- Structures of the EphA2 Receptor at the Membrane: Role of Lipid Interactions.Structure (London, England : 1993) · 2016Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Integrins are large cell-surface adhesion receptors that can be activated to a high affinity state by the formation of an intracellular complex between the integrin β-subunit tail, the membrane, and talin. The F2 and F3 subdomains of the talin head play a key role in formation of this complex. Here, activation of the integrin αIIb/β3 dimer by the talin head domain was probed using multiscale molecular dynamics simulations. A number of novel insights emerge from these studies, including (i) the importance of the integrin αIIb subunit F992 and F993 residues in stabilizing the "off" state of the αIIb/β3 dimer, (ii) a crucial role for negatively charged groups in the F2-F3/membrane interaction, (iii) binding of the talin F2-F3 domain to negatively charged lipid headgroups in the membrane induces a reorientation of the β transmembrane (TM) domain, (iv) an increase in the tilt angle of the β TM domain relative to the bilayer normal helps to destabilize the α/β TM interaction and promote a scissor-like movement of the integrin TM helices. These results, combined with various published experimental observations, suggest a model for the mechanism of inside-out activation of integrins by talin.
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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.