Opsin is a phospholipid flippase. Academic Article uri icon

Overview

MeSH

  • Adenosine Triphosphate
  • Animals
  • Cattle
  • Gene Expression Regulation
  • HEK293 Cells
  • Humans
  • Membrane Proteins
  • Photoreceptor Cells, Vertebrate

MeSH Major

  • Opsins
  • Phospholipids

abstract

  • Polar lipids must flip-flop rapidly across biological membranes to sustain cellular life [1, 2], but flipping is energetically costly [3] and its intrinsic rate is low. To overcome this problem, cells have membrane proteins that function as lipid transporters (flippases) to accelerate flipping to a physiologically relevant rate. Flippases that operate at the plasma membrane of eukaryotes, coupling ATP hydrolysis to unidirectional lipid flipping, have been defined at a molecular level [2]. On the other hand, ATP-independent bidirectional flippases that translocate lipids in biogenic compartments, e.g., the endoplasmic reticulum, and specialized membranes, e.g., photoreceptor discs [4, 5], have not been identified even though their activity has been recognized for more than 30 years [1]. Here, we demonstrate that opsin is the ATP-independent phospholipid flippase of photoreceptor discs. We show that reconstitution of opsin into large unilamellar vesicles promotes rapid (τ<10 s) flipping of phospholipid probes across the vesicle membrane. This is the first molecular identification of an ATP-independent phospholipid flippase in any system. It reveals an unexpected activity for opsin and, in conjunction with recently available structural information on this G protein-coupled receptor [6, 7], significantly advances our understanding of the mechanism of ATP-independent lipid flip-flop. Copyright © 2011 Elsevier Ltd. All rights reserved.

publication date

  • January 25, 2011

has subject area

  • Adenosine Triphosphate
  • Animals
  • Cattle
  • Gene Expression Regulation
  • HEK293 Cells
  • Humans
  • Membrane Proteins
  • Opsins
  • Phospholipids
  • Photoreceptor Cells, Vertebrate

Research

keywords

  • Journal Article

Identity

Language

  • eng

PubMed Central ID

  • PMC3057128

Digital Object Identifier (DOI)

  • 10.1016/j.cub.2010.12.031

PubMed ID

  • 21236677

Additional Document Info

start page

  • 149

end page

  • 153

volume

  • 21

number

  • 2