ArticleProceedings of the National Academy of Sciences of the United States of America2012
Affinity of talin-1 for the β3-integrin cytosolic domain is modulated by its phospholipid bilayer environment.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 66 citations in OpenAlex.
- The structure of an amyloid precursor protein/talin complex indicates a mechanical basis of Alzheimer's disease.Open biology · 2024Article
- High-resolution snapshots of the talin auto-inhibitory states suggest roles in cell adhesion and signaling.Nature communications · 2024Article
- Talin and kindlin use integrin tail allostery and direct binding to activate integrins.Nature structural & molecular biology · 2023Article
- Review
- Intrinsically disordered region of talin's FERM domain functions as an initial PIPBiophysical journal · 2023Article
- Talin variant P229S compromises integrin activation and associates with multifaceted clinical symptoms.Human molecular genetics · 2022Article
- PI(4,5)P2: signaling the plasma membrane.The Biochemical journal · 2022Article
- Integrin Regulators in Neutrophils.Cells · 2022Review
- Mechanism of integrin activation by talin and its cooperation with kindlin.Nature communications · 2022Article
- Review of PIP2 in Cellular Signaling, Functions and Diseases.International journal of molecular sciences · 2020Review
- The F1 loop of the talin head domain acts as a gatekeeper in integrin activation and clustering.Journal of cell science · 2020Article
- Structural basis of Focal Adhesion Kinase activation on lipid membranes.The EMBO journal · 2020Article
- A distinct talin2 structure directs isoform specificity in cell adhesion.The Journal of biological chemistry · 2020Article
- GIV•Kindlin Interaction Is Required for Kindlin-Mediated Integrin Recognition and Activation.iScience · 2020Article
- Molecular mechanism for bidirectional regulation of CD44 for lipid raft affiliation by palmitoylations and PIP2.PLoS computational biology · 2020Article
- Talin and Kindlin as Integrin-Activating Proteins: Focus on the Heart.Pediatric cardiology · 2019Review
- Filopodia and focal adhesions: An integrated system driving branching morphogenesis in neuronal pathfinding and angiogenesis.Developmental biology · 2019Review
- Article
- LCP1 preferentially binds clasped αMβ2 integrin and attenuates leukocyte adhesion under flow.Journal of cell science · 2018Article
- Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Binding of the talin-1 FERM (4.1/ezrin/radixin/moesin) domain to the β3 cytosolic tail causes activation of the integrin αIIbβ3. The FERM domain also binds to acidic phospholipids. Although much is known about the interaction of talin-1 with integrins and lipids, the relative contribution of each interaction to integrin regulation and possible synergy between them remain to be clarified. Here, we examined the thermodynamic interplay between FERM domain binding to phospholipid bilayers and to its binding sites in the β3 tail. We found that although both the F0F1 and F2F3 subdomains of the talin-1 FERM domain bind acidic bilayers, the full-length FERM domain binds with an affinity similar to F2F3, indicating that F0F1 contributes little to the overall interaction. When free in solution, the β3 tail has weak affinity for the FERM domain. However, appending the tail to acidic phospholipids increased its affinity for the FERM domain by three orders of magnitude. Nonetheless, the affinity of the FERM for the appended tail was similar to its affinity for binding to bilayers alone. Thus, talin-1 binding to the β3 tail is a ternary interaction dominated by a favorable surface interaction with phospholipid bilayers and set by lipid composition. Nonetheless, interactions between the FERM domain, the β3 tail, and lipid bilayers are not optimized for a high-affinity synergistic interaction, even at the membrane surface. Instead, the interactions appear to be tuned in such a way that the equilibrium between inactive and active integrin conformations can be readily regulated.
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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.