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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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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The BAR domain is known as a binding platform for several protein-protein interactions.
“However, the BAR domain is also known as a binding platform for several protein-protein interactions (37,38), suggesting that BACE1 is a novel cargo protein of BIN1 that is sorted from early endosomes to late endosomes/lysosomes.”
From BIN1 regulates BACE1 intracellular trafficking and amyloid-β production (2016) · cites this paper as [37]
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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
- Published
- 2004-03-01
- Volume
- 5
- Issue
- 3
- Pages
- 250-255
- ISSN
- 1469-221X (ISSN-L)
- 1469-3178
- 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
- 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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