BAR, F-BAR (EFC) and ENTH/ANTH domains in the regulation of membrane-cytosol interfaces and membrane curvature.
Abstract
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.
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Yeast two-hybrid screens with PSD-95 identified RalBP1 as a novel PSD-95-interacting protein.
“Yeast two-hybrid screens with PSD-95 identified RalBP1 as a novel PSD-95-interacting protein, which is coupled to other endocytic proteins including POB1, RalA, AP2, epsin, and Eps15 (Figure 1A) [34],[36].”
From Regulated RalBP1 Binding to RalA and PSD-95 Controls AMPA Receptor Endocytosis and LTD (2009) · cites this paper as [36]
AP2 and POB1 further associate with EH domain-containing endocytic proteins epsin and Eps15.
“which further associate with EH domain-containing endocytic proteins epsin and Eps15 [36].”
From Regulated RalBP1 Binding to RalA and PSD-95 Controls AMPA Receptor Endocytosis and LTD (2009) · cites this paper as [36]
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- Authors
- ITOH, T., & DECAMILLI, P.
- Affiliations
- Howard Hughes Medical Institute (US)
- Corresponding author
- DECAMILLI, P
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids
- Publisher
- Elsevier BV
- Published
- 2006-08
- Volume
- 1761
- Issue
- 8
- Pages
- 897-912
- ISSN
- 1388-1981 (ISSN-L)
- OpenAlex
- W1990380758
- Cited by
- 361
- References
- 5
- Citations by year
- 2026: 4 · 2025: 5 · 2024: 3 · 2023: 10 · 2022: 6 · 2021: 14 · 2020: 9 · 2019: 12 · 2018: 10 · 2017: 13 · 2016: 12 · 2015: 17 · 2014: 25 · 2013: 14 · 2012: 25
- FWCI
- 15.55
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Yale University
- National Institutes of Health
- National Institute on Drug Abuse (DA 018343, P30DA018343)
- National Cancer Institute (P01CA046128, CA46128)
- National Institute of Neurological Disorders and Stroke (NS36251)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Caveolin-1 and cellular processes
- Keywords
- BAR domain, ENTH domain, F-BAR domain, membrane curvature, membrane deformation, amphipathic helix, lipid bilayer binding, membrane budding, endocytosis, curvature sensing
- MeSH terms
- Actins, Acyltransferases, Animals, Cell Membrane, Chlorocebus aethiops, Cytosol, Endocytosis, Lipid Bilayers, Membrane Lipids, Models, Molecular, Nerve Tissue Proteins, Phosphatidylinositols, Protein Binding, Protein Structure, Tertiary, COS Cells, GTP Phosphohydrolases, Adaptor Proteins, Vesicular Transport
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