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

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ELSEVIER
DOI: 10.1016/j.bbalip.2006.06.015

Keywords

PCH family; EFC domain; FCH domain; IMD domain; dynamin; clathrin; N-WASP; tubulation; actin; endocytosis

Funding

  1. NCI NIH HHS [CA46128] Funding Source: Medline
  2. NIDA NIH HHS [P30 DA018343, DA018343] Funding Source: Medline
  3. NINDS NIH HHS [NS36251] Funding Source: Medline

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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. (c) 2006 Elsevier B.V. All rights reserved.

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