BAR, F-BAR (EFC) and ENTH/ANTH domains in the regulation of membrane-cytosol interfaces and membrane curvature

Biochim Biophys Acta. 2006 Aug;1761(8):897-912. doi: 10.1016/j.bbalip.2006.06.015. Epub 2006 Jul 28.


BAR and ENTH domains are families of alpha-helical lipid bilayer binding modules found in proteins that function in endocytosis, actin regulation and signaling. Several members of these families not only bind the bilayer, but also participate in the regulation of its curvature. These properties are thought to play physiological roles at sites of membrane budding and at other sites where narrow tubular membranes occur in vivo. Studies of BAR and ENTH domains and of their flanking regions have provided new insights into mechanisms of membrane deformation and curvature sensing, and have emphasized the importance of amphipathic helices, thought to intercalate in one of the leaflets of the lipid bilayer, in the generation of membrane curvature. Structural studies and database searches are rapidly expanding the BAR and ENTH domains families, with the identification of new related domains and subfamilies, such as F-BAR (also called EFC) domains and ANTH domains, respectively. Here we present a short overview of the properties of these domains based on evidence obtained from genetics, cell biology, biochemistry and structural biology.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Actins / metabolism
  • Acyltransferases / chemistry
  • Acyltransferases / genetics
  • Adaptor Proteins, Vesicular Transport / chemistry
  • Adaptor Proteins, Vesicular Transport / genetics
  • Animals
  • COS Cells
  • Cell Membrane / chemistry*
  • Cell Membrane / metabolism
  • Chlorocebus aethiops
  • Cytosol / chemistry*
  • Cytosol / metabolism
  • Endocytosis*
  • GTP Phosphohydrolases / chemistry
  • Lipid Bilayers / chemistry*
  • Lipid Bilayers / metabolism
  • Membrane Lipids / chemistry
  • Models, Molecular
  • Nerve Tissue Proteins / chemistry
  • Nerve Tissue Proteins / genetics
  • Phosphatidylinositols / chemistry
  • Protein Binding
  • Protein Structure, Tertiary*


  • Actins
  • Adaptor Proteins, Vesicular Transport
  • Lipid Bilayers
  • Membrane Lipids
  • Nerve Tissue Proteins
  • Phosphatidylinositols
  • epsin
  • amphiphysin
  • Acyltransferases
  • 2-acylglycerophosphate acyltransferase
  • GTP Phosphohydrolases