Lipid flippases and their biological functions. Review uri icon

Overview

MeSH

  • Adenosine Triphosphatases
  • Biological Transport, Active
  • Endoplasmic Reticulum
  • Glycerophospholipids
  • Intracellular Membranes
  • Models, Biological
  • Models, Molecular
  • Transport Vesicles

MeSH Major

  • ATP-Binding Cassette Transporters
  • Lipid Metabolism
  • Lipids
  • Phospholipid Transfer Proteins

abstract

  • The typically distinct phospholipid composition of the two leaflets of a membrane bilayer is generated and maintained by bi-directional transport (flip-flop) of lipids between the leaflets. Specific membrane proteins, termed lipid flippases, play an essential role in this transport process. Energy-independent flippases allow common phospholipids to equilibrate rapidly between the two monolayers and also play a role in the biosynthesis of a variety of glycoconjugates such as glycosphingolipids, N-glycoproteins, and glycosylphosphatidylinositol (GPI)-anchored proteins. ATP-dependent flippases, including members of a conserved subfamily of P-type ATPases and ATP-binding cassette transporters, mediate the net transfer of specific phospholipids to one leaflet of a membrane and are involved in the creation and maintenance of transbilayer lipid asymmetry of membranes such as the plasma membrane of eukaryotes. Energy-dependent flippases also play a role in the biosynthesis of glycoconjugates such as bacterial lipopolysaccharide. This review summarizes recent progress on the identification and characterization of the various flippases and the demonstration of their biological functions.

publication date

  • December 2006

has subject area

  • ATP-Binding Cassette Transporters
  • Adenosine Triphosphatases
  • Biological Transport, Active
  • Endoplasmic Reticulum
  • Glycerophospholipids
  • Intracellular Membranes
  • Lipid Metabolism
  • Lipids
  • Models, Biological
  • Models, Molecular
  • Phospholipid Transfer Proteins
  • Transport Vesicles

Research

keywords

  • Journal Article
  • Review

Identity

Language

  • eng

Digital Object Identifier (DOI)

  • 10.1007/s00018-006-6167-7

PubMed ID

  • 17103115

Additional Document Info

start page

  • 2908

end page

  • 2921

volume

  • 63

number

  • 24