ArticleThe Journal of biological chemistry2015
Annular anionic lipids stabilize the integrin αIIbβ3 transmembrane complex.
Article in The Journal of biological chemistry, 2015. 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.
- Comparison of Integrin αIIbβ3 Transmembrane Association in Vesicles and Bicelles.Biochemistry · 2023Article
- Dynamic lipid turnover in photoreceptors and retinal pigment epithelium throughout life.Progress in retinal and eye research · 2022Review
- The binding of autotaxin to integrins mediates hyperhomocysteinemia-potentiated platelet activation and thrombosis in mice and humans.Blood advances · 2022Article
- Reconstitution of Functional Integrin αIIbβ3 and Its Activation in Plasma Membrane-Mimetic Lipid Environments.Membranes · 2021Article
- Insight Into Pathological Integrin αIIbβ3 Activation From Safeguarding The Inactive State.Journal of molecular biology · 2021Article
- Fluorescence Correlation Spectroscopy Reveals Interaction of Some Microdomain-Associated Lipids with Cellular Focal Adhesion Sites.International journal of molecular sciences · 2020Article
- Multiscale Simulations of Biological Membranes: The Challenge To Understand Biological Phenomena in a Living Substance.Chemical reviews · 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
- Intramembrane ionic protein-lipid interaction regulates integrin structure and function.PLoS biology · 2018Article
- On the contributing role of the transmembrane domain for subunit-specific sensitivity of integrin activation.Scientific reports · 2018Article
- Membrane Anchoring of α-Helical Proteins: Role of Tryptophan.The journal of physical chemistry. B · 2018Article
- The Integrin Receptor in Biologically Relevant Bilayers: Insights from Molecular Dynamics Simulations.The Journal of membrane biology · 2017Article
- Structure and lipid-binding properties of the kindlin-3 pleckstrin homology domain.The Biochemical journal · 2017Article
- Article
- Direct Evaluation of Protein-Lipid Contacts Reveals Protein Membrane Immersion and Isotropic Bicelle Structure.The journal of physical chemistry letters · 2016Article
- A Conserved Ectodomain-Transmembrane Domain Linker Motif Tunes the Allosteric Regulation of Cell Surface Receptors.The Journal of biological chemistry · 2016Article
- Structural and thermodynamic basis of proline-induced transmembrane complex stabilization.Scientific reports · 2016Article
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Authors and funding
7 authors.
Funding
Abstract
Cationic membrane-proximal amino acids determine the topology of membrane proteins by interacting with anionic lipids that are restricted to the intracellular membrane leaflet. This mechanism implies that anionic lipids interfere with electrostatic interactions of membrane proteins. The integrin αIIbβ3 transmembrane (TM) complex is stabilized by a membrane-proximal αIIb(Arg(995))-β3(Asp(723)) interaction; here, we examine the influence of anionic lipids on this complex. Anionic lipids compete for αIIb(Arg(995)) contacts with β3(Asp(723)) but paradoxically do not diminish the contribution of αIIb(Arg(995))-β3(Asp(723)) to TM complex stability. Overall, anionic lipids in annular positions stabilize the αIIbβ3 TM complex by up to 0.50 ± 0.02 kcal/mol relative to zwitterionic lipids in a headgroup structure-dependent manner. Comparatively, integrin receptor activation requires TM complex destabilization of 1.5 ± 0.2 kcal/mol, revealing a sizeable influence of lipid composition on TM complex stability. We implicate changes in lipid headgroup accessibility to small molecules (physical membrane characteristics) and specific but dynamic protein-lipid contacts in this TM helix-helix stabilization. Thus, anionic lipids in ubiquitous annular positions can benefit the stability of membrane proteins while leaving membrane-proximal electrostatic interactions intact.
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