ArticleStructure (London, England : 1993)2018
Mechanisms of Lipid Scrambling by the G Protein-Coupled Receptor Opsin.
Article in Structure (London, England : 1993), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 72 citations in OpenAlex.
- Article
- Article
- Sequence constraints predispose Class D GPCRs to follow an atypical activation mechanism.bioRxiv : the preprint server for biology · 2026Article
- AI-guided transition path sampling of lipid flip-flop and membrane nanoporation.Nature communications · 2025Article
- Mechanism of Phosphatidylserine Lipid Scrambling by Human SERINC3, an HIV-1 Restriction Factor.bioRxiv : the preprint server for biology · 2025Article
- Opsins are Phospholipid Scramblases in All Domains of Life.bioRxiv : the preprint server for biology · 2025Article
- Lipid Scrambling Pathways in the Sec61 Translocon Complex.Journal of the American Chemical Society · 2025Article
- TMEM16 and OSCA/TMEM63 proteins share a conserved potential to permeate ions and phospholipids.eLife · 2024Article
- TMEM16 and OSCA/TMEM63 proteins share a conserved potential to permeate ions and phospholipids.bioRxiv : the preprint server for biology · 2024Article
- Insertases scramble lipids: Molecular simulations of MTCH2.Structure (London, England : 1993) · 2024Article
- A cholesterol switch controls phospholipid scrambling by G protein-coupled receptors.The Journal of biological chemistry · 2024Article
- Insertases Scramble Lipids: Molecular Simulations of MTCH2.bioRxiv : the preprint server for biology · 2023Article
- Article
- The allosteric mechanism leading to an open-groove lipid conductive state of the TMEM16F scramblase.Communications biology · 2022Article
- Cholesterol occupies the lipid translocation pathway to block phospholipid scrambling by a G protein-coupled receptor.Structure (London, England : 1993) · 2022Article
- Phospholipid Scrambling by G Protein-Coupled Receptors.Annual review of biophysics · 2022Review
- A Fluorescence-based Assay for Measuring Phospholipid Scramblase Activity in Giant Unilamellar Vesicles.Bio-protocol · 2022Article
- Rethinking Opsins.Molecular biology and evolution · 2022Article
- The tertiary structure of the human Xkr8-Basigin complex that scrambles phospholipids at plasma membranes.Nature structural & molecular biology · 2021Article
- Cryo-EM structures of the caspase-activated protein XKR9 involved in apoptotic lipid scrambling.eLife · 2021Article
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6 authors at 2 institutions in 2 countries.
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Abstract
Several class-A G protein-coupled receptor (GPCR) proteins act as constitutive phospholipid scramblases catalyzing the transbilayer translocation of >10,000 phospholipids per second when reconstituted into synthetic vesicles. To address the molecular mechanism by which these proteins facilitate rapid lipid scrambling, we carried out large-scale ensemble atomistic molecular dynamics simulations of the opsin GPCR. We report that, in the process of scrambling, lipid head groups traverse a dynamically revealed hydrophilic pathway in the region between transmembrane helices 6 and 7 of the protein while their hydrophobic tails remain in the bilayer environment. We present quantitative kinetic models of the translocation process based on Markov State Model analysis. As key residues on the lipid translocation pathway are conserved within the class-A GPCR family, our results illuminate unique aspects of GPCR structure and dynamics while providing a rigorous basis for the design of variants of these proteins with defined scramblase activity.
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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.