Constitutive phospholipid scramblase activity of a G protein-coupled receptor

Michael A. Goren, Takefumi Morizumi, Indu Menon, Jeremiah S. Joseph, Jeremy S. Dittman, Vadim Cherezov, Raymond C. Stevens, Oliver P. Ernst and Anant K. Menon ()
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Michael A. Goren: Weill Cornell Medical College
Takefumi Morizumi: University of Toronto
Indu Menon: Weill Cornell Medical College
Jeremiah S. Joseph: The Scripps Research Institute
Jeremy S. Dittman: Weill Cornell Medical College
Vadim Cherezov: The Scripps Research Institute
Raymond C. Stevens: The Scripps Research Institute
Oliver P. Ernst: University of Toronto
Anant K. Menon: Weill Cornell Medical College

Nature Communications, 2014, vol. 5, issue 1, 1-10

Abstract: 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.

Date: 2014
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DOI: 10.1038/ncomms6115

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