ArticleScientific reports2017
An engineered opsin monomer scrambles phospholipids.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 17 citations in OpenAlex.
- A single-vesicle fluorescence microscopy platform to quantify phospholipid scrambling.Nature structural & molecular biology · 2026Article
- A single vesicle fluorescence microscopy platform to quantify phospholipid scrambling.bioRxiv : the preprint server for biology · 2025Article
- A cholesterol switch controls phospholipid scrambling by G protein-coupled receptors.The Journal of biological chemistry · 2024Article
- Phospholipid Scrambling by G Protein-Coupled Receptors.Annual review of biophysics · 2022Review
- Endoplasmic reticulum phospholipid scramblase activity revealed after protein reconstitution into giant unilamellar vesicles containing a photostable lipid reporter.Scientific reports · 2021Article
- Unusual mode of dimerization of retinitis pigmentosa-associated F220C rhodopsin.Scientific reports · 2021Article
- Complexity of the eukaryotic dolichol-linked oligosaccharide scramblase suggested by activity correlation profiling mass spectrometry.Scientific reports · 2021Article
- Article
- Scrambling of natural and fluorescently tagged phosphatidylinositol by reconstituted G protein-coupled receptor and TMEM16 scramblases.The Journal of biological chemistry · 2018Article
- Structural mapping of fluorescently-tagged, functional nhTMEM16 scramblase in a lipid bilayer.The Journal of biological chemistry · 2018Article
- Out-of-the-groove transport of lipids by TMEM16 and GPCR scramblases.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The G protein-coupled receptor opsin is a phospholipid scramblase that facilitates rapid transbilayer phospholipid exchange in liposomes. The mechanism by which opsin scrambles lipids is unknown. It has been proposed that lipid translocation may occur at protein-protein interfaces of opsin dimers. To test this possibility, we rationally engineered QUAD opsin by tryptophan substitution of four lipid-facing residues in transmembrane helix 4 (TM4) that is known to be important for dimerization. Atomistic molecular dynamics simulations of wild type and QUAD opsins combined with continuum modeling revealed that the tryptophan substitutions lower the energetically unfavorable residual hydrophobic mismatch between TM4 and the membrane, reducing the drive of QUAD opsin to dimerize. We purified thermostable wild type and QUAD opsins, with or without a SNAP tag for fluorescence labeling. Single molecule fluorescence measurements of purified SNAP-tagged constructs revealed that both proteins are monomers. Fluorescence-based activity assays indicated that QUAD opsin is a fully functional scramblase. However, unlike wild type opsin which dimerizes en route to insertion into phospholipid vesicles, QUAD opsin reconstitutes as a monomer. We conclude that an engineered opsin monomer can scramble phospholipids, and that the lipid-exposed face of TM4 is unlikely to contribute to transbilayer phospholipid exchange.
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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.