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- W1993460406 abstract "Opsin, the rhodopsin apoprotein, was recently shown to be an ATP-independent flippase (or scramblase) that equilibrates phospholipids across photoreceptor disc membranes in mammalian retina, a process required for disc homoeostasis. Here we show that scrambling is a constitutive activity of rhodopsin, distinct from its light-sensing function. Upon reconstitution into vesicles, discrete conformational states of the protein (rhodopsin, a metarhodopsin II-mimic, and two forms of opsin) facilitated rapid (>10,000 phospholipids per protein per second) scrambling of phospholipid probes. Our results indicate that the large conformational changes involved in converting rhodopsin to metarhodopsin II are not required for scrambling, and that the lipid translocation pathway either lies near the protein surface or involves membrane packing defects in the vicinity of the protein. In addition, we demonstrate that β2-adrenergic and adenosine A2A receptors scramble lipids, suggesting that rhodopsin-like G protein-coupled receptors may play an unexpected moonlighting role in re-modelling cell membranes." @default.
- W1993460406 created "2016-06-24" @default.
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- W1993460406 date "2014-10-08" @default.
- W1993460406 modified "2023-10-14" @default.
- W1993460406 title "Constitutive phospholipid scramblase activity of a G protein-coupled receptor" @default.
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- W1993460406 doi "https://doi.org/10.1038/ncomms6115" @default.
- W1993460406 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4198942" @default.
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- W1993460406 hasPublicationYear "2014" @default.
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