Amphipathic helices and membrane curvature

FEBS Lett. 2010 May 3;584(9):1840-7. doi: 10.1016/j.febslet.2009.10.022. Epub 2009 Oct 20.

Abstract

Numerous data have been collected on lipid-binding amphipathic helices involved in membrane-remodeling machineries and vesicular transport. Here we describe how, with regard to lipid composition, the physicochemical features of some amphipathic helices explain their ability to recognize membrane curvature or to participate in membrane remodeling. We propose that sensing highly-curved membranes requires that the polar and hydrophobic faces of the helix do not cooperate in lipid binding. A more detailed description of the interaction between amphipathic helices and lipids is however needed; notably to explain how new helices contribute to detection of modest changes in curvature or even negative curvature.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence / physiology
  • Animals
  • Cell Membrane / chemistry
  • Cell Membrane / physiology*
  • Cell Membrane / ultrastructure
  • Humans
  • Hydrophobic and Hydrophilic Interactions
  • Membrane Fluidity / physiology*
  • Membrane Lipids / chemistry
  • Membrane Lipids / metabolism
  • Membrane Proteins / chemistry*
  • Membrane Proteins / physiology
  • Models, Biological
  • Models, Molecular
  • Protein Folding
  • Protein Structure, Secondary / physiology*

Substances

  • Membrane Lipids
  • Membrane Proteins