Cited by 282Cellular transport and secretionProtein Kinase Regulation and GTPase SignalingLipid Membrane Structure and Behavior

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The BAR‐domain family of proteins: a case of bending and binding?: The membrane bending and GTPase-binding functions of proteins from the BAR-domain family

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Habermann, Bianca·2004·The EMBO Reports

DOI 10.1038/sj.embor.7400105PMC PMC1299016

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Abstract

BAR-domains recently took centre stage in science through a report on the crystal structure of this domain in Drosophila Amphiphysin. Though only weakly conserved at the sequence level, the structure of the BAR domain shows striking similarity to the GTPase-binding domain of Arfaptin 2, an effector of Rho- and Arf- GTPases. On the basis of this sequence and structural similarity, these two proteins have been classified as belonging to the same family, the BAR-domain family, and they probably also have similar functional characteristics. Presented here are the results of a database search for the sequence of the BAR domain of Amphiphysin and Arfaptin 2. This search identified a variety of related proteins, most of which are involved in intracellular transport and especially in endocytosis. For example, the BAR-domain family includes Endophilins, GTPase-activating proteins of the Centaurinbeta family and Oligophrenins, the adaptor proteins APPL1 and APPL2 that were recently shown to interact with the small GTPase Rab5, as well as members of the Sorting nexin family. On the basis of the structures of Amphiphysin and Arfaptin 2 and the cellular role of Amphiphysins in the early steps of endocytosis, the functions of the BAR domain have been defined as a dimerization motif and as sensing and inducing membrane curvature. However, data on Arfaptin 2 and now also on the Adaptor proteins APPL1 and 2 suggest that another function of the BAR domain is to bind to small GTPases.

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Authors: Habermann, B.
Affiliations: Max Planck Institute of Molecular Cell Biology and Genetics (DE)
Corresponding author: Habermann, Bianca
ORCID: Habermann, Bianca
Venue: The EMBO Reports
Publisher: Springer Science and Business Media LLC
Published: 2004-03-01
Volume: 5
Issue: 3
Pages: 250-255
ISSN: 1469-221X (ISSN-L)
1469-3178
DOI: 10.1038/sj.embor.7400105
PMC: PMC1299016
OpenAlex: W2151624014
Cited by: 281
References: 24
Citations by year: 2026: 1 · 2025: 5 · 2024: 6 · 2023: 8 · 2022: 10 · 2021: 11 · 2020: 9 · 2019: 7 · 2018: 8 · 2017: 6 · 2016: 4 · 2015: 7 · 2014: 14 · 2013: 9 · 2012: 19
FWCI: 9.95
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: EMBO Reports (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
Keywords: BAR domain, amphiphysin, protein family classification, GTPase-binding domain, membrane curvature, endocytosis, intracellular transport, Rab5, APPL1, APPL2, sorting nexins, endophilin
MeSH terms: Amino Acid Sequence, Animals, Cell Membrane, Drosophila, Endocytosis, Molecular Sequence Data, Nerve Tissue Proteins, Phylogeny, Protein Conformation, Sequence Alignment, Protein Structure, Tertiary, Dimerization, GTP-Binding Protein Regulators, Monomeric GTP-Binding Proteins, Adaptor Proteins, Signal Transducing

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The BAR‐domain family of proteins: a case of bending and binding?: The membrane bending and GTPase-binding functions of proteins from the BAR-domain family

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