ArticleBiochimica et biophysica acta2016
Conformational equilibrium of talin is regulated by anionic lipids.
Article in Biochimica et biophysica acta, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 25 citations in OpenAlex.
- Design of Fluorescent Membrane Scaffold Proteins for Nanodiscs.bioRxiv : the preprint server for biology · 2026Article
- Examining the thermotropic properties of large circularized nanodiscs.Biochimica et biophysica acta. Biomembranes · 2025Article
- Membrane-induced 2D phase separation of the focal adhesion protein talin.Nature communications · 2024Article
- Long-term depression in neurons involves temporal and ultra-structural dynamics of phosphatidylinositol-4,5-bisphosphate relying on PIP5K, PTEN and PLC.Communications biology · 2023Article
- Structures and Dynamics of Anionic Lipoprotein Nanodiscs.The journal of physical chemistry. B · 2022Article
- Nanodiscs: A toolkit for membrane protein science.Protein science : a publication of the Protein Society · 2021Review
- CLIC1 recruits PIP5K1A/C to induce cell-matrix adhesions for tumor metastasis.The Journal of clinical investigation · 2021Article
- Dark, Ultra-Dark and Ultra-Bright Nanodiscs for membrane protein investigations.Analytical biochemistry · 2020Article
- Nanodisc self-assembly is thermodynamically reversible and controllable.Soft matter · 2020Article
- Molecular Orientation Determination in Nanodiscs at the Single-Molecule Level.Analytical chemistry · 2020Article
- Emerging Diversity in Lipid-Protein Interactions.Chemical reviews · 2019Review
- The hydrodynamic motion of Nanodiscs.Chemistry and physics of lipids · 2019Article
- Regulation of actin assembly by PI(4,5)P2 and other inositol phospholipids: An update on possible mechanisms.Biochemical and biophysical research communications · 2018Review
- Nanodiscs: A Controlled Bilayer Surface for the Study of Membrane Proteins.Annual review of biophysics · 2018Article
- Nanodiscs in Membrane Biochemistry and Biophysics.Chemical reviews · 2017Review
- Bax transmembrane domain interacts with prosurvival Bcl-2 proteins in biological membranes.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Gα13 Switch Region 2 Relieves Talin Autoinhibition to Activate αIIbβ3 Integrin.The Journal of biological chemistry · 2016Article
- Phosphatidylinositol 4,5-Bisphosphate Modulates the Affinity of Talin-1 for Phospholipid Bilayers and Activates Its Autoinhibited Form.Biochemistry · 2016Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
A critical step in the activation of integrin receptors is the binding of talin to the cytoplasmic domain of the β subunits. This interaction leads to separation of the integrin α and β transmembrane domains and significant conformational changes in the extracellular domains, resulting in a dramatic increase in integrin's affinity for ligands. It has long been shown that the membrane bilayer also plays a critical role in the talin-integrin interaction. Anionic lipids are required for proper interaction, yet the specificity for specific anionic headgroups is not clear. In this report, we document talin-membrane interactions with bilayers of controlled composition using Nanodiscs and a FRET based binding and structural assay. We confirm that recruitment of the talin head domain to the membrane surface is governed by charge in the absence of other adapter proteins. In addition, measurement of the donor-acceptor distance is consistent with the hypothesis that anionic lipids promote a conformational change in the talin head domain allowing interaction of the F3 domain with the phospholipid bilayer. The magnitude of the F3 domain movement is altered by the identity of the phospholipid headgroup with phosphatidylinositides promoting the largest change. Our results suggest that phoshpatidylinositol-4,5-bisphosphate plays key a role in converting talin head domain to a conformation optimized for interactions with the bilayer and subsequently integrin cytoplasmic tails.
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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.