BAR domain explained
| Symbol: | BAR |
| BAR domain |
| Pfam: | PF03114 |
| Interpro: | IPR004148 |
| Smart: | SM00721 |
| Prosite: | PDOC51021 |
| Scop: | 1uru |
| Cdd: | cd07307 |
| Symbol: | BAR-2 |
| Bin/amphiphysin/Rvs domain |
| Pfam: | PF10455 |
| Symbol: | BAR-3 |
| BAR domain of APPL family |
| Pfam: | PF16746 |
| Symbol: | FCH |
| EFC/F-BAR homology domain |
| Pfam: | PF00611 |
| Symbol: | BAR-3-WASP |
| WASP-binding domain of sorting nexin proteins |
| Pfam: | PF10456 |
In molecular biology, BAR domains are highly conserved protein dimerisation domains that occur in many proteins involved in membrane dynamics in a cell. The BAR domain is banana-shaped and binds to membrane via its concave face. It is capable of sensing membrane curvature by binding preferentially to curved membranes. BAR domains are named after three proteins that they are found in: Bin, Amphiphysin and Rvs.
BAR domains occur in combinations with other domains
Many BAR family proteins contain alternative lipid specificity domains that help target these protein to particular membrane compartments. Some also have SH3 domains that bind to dynamin and thus proteins like amphiphysin and endophilin are implicated in the orchestration of vesicle scission.
N-BAR domain
Some BAR domain containing proteins have an N-terminal amphipathic helix preceding the BAR domain. This helix inserts (like in the epsin ENTH domain) into the membrane and induces curvature, which is stabilised by the BAR dimer. Amphiphysin, endophilin, BRAP1/bin2 and nadrin are examples of such proteins containing an N-BAR. The Drosophila amphiphysin N-BAR (DA-N-BAR) is an example of a protein with a preference for negatively charged surfaces.
Human proteins containing this domain
AMPH
- ARHGAP17; ARHGAP44; BIN1; BIN2; BIN3;SH3BP1
SH3GL1; SH3GL2; SH3GL3; SH3GLB1; SH3GLB2.[1]
F-BAR (EFC) domain
F-BAR domains (for FCH-BAR, or EFC for Extended FCH Homology) are BAR domains that are extensions of the already established FCH domain. They are frequently found at the amino terminus of proteins. They can bind lipid membranes and can tubulate lipids in vitro and in vivo, but their exact physiological role still is under investigation.[2] Examples of the F-BAR domain family are CIP4/FBP17/Toca-1, Syndapins (also called PACSINs) and muniscins. Gene knock-out of syndapin I in mice revealed that this brain-enriched isoform of the syndapin family is crucial for proper size control of synaptic vesicles and thereby indeed helps to define membrane curvature a physiological process. Work of the lab of Britta Qualmann also demonstrated that syndapin I is crucial for proper targeting of the large GTPase dynamin to membranes.[3]
Sorting nexins
The sorting nexin family of proteins includes several members that possess a BAR domain, including the well characterized SNX1 and SNX9.
Human proteins containing this domain
AMPH
- ARHGAP17; BIN1; BIN2; BIN3; DNMBP; GMIP; RICH2; SH3BP1;SH3GL1
SH3GL2; SH3GL3; SH3GLB1; SH3GLB2;
See also
External links
References
Further reading
- Leventis PA, Chow BM, Stewart BA, Iyengar B, Campos AR, Boulianne GL . Drosophila Amphiphysin is a post-synaptic protein required for normal locomotion but not endocytosis . . 2 . 11 . 839–50 . November 2001 . 11733051 . 10.1034/j.1600-0854.2001.21113.x .
- Zhang B, Zelhof AC . Amphiphysins: raising the BAR for synaptic vesicle recycling and membrane dynamics. Bin-Amphiphysin-Rvsp . . 3 . 7 . 452–60 . July 2002 . 12047553 . 10.1034/j.1600-0854.2002.30702.x . Review.
- Zelhof AC, Bao H, Hardy RW, Razzaq A, Zhang B, Doe CQ . Drosophila Amphiphysin is implicated in protein localization and membrane morphogenesis but not in synaptic vesicle endocytosis . . 128 . 24 . 5005–15 . December 2001 . 10.1242/dev.128.24.5005 . 11748137 .
- Mathew D, Popescu A, Budnik V . Drosophila amphiphysin functions during synaptic Fasciclin II membrane cycling . . 23 . 33 . 10710–6 . November 2003 . 14627656 . 6740931 . 10.1523/JNEUROSCI.23-33-10710.2003.
- Peter BJ, Kent HM, Mills IG . BAR domains as sensors of membrane curvature: the amphiphysin BAR structure . Science . 303 . 5657 . 495–9 . January 2004 . 14645856 . 10.1126/science.1092586 . 6104655 . etal. free .
- Weissenhorn W . Crystal structure of the endophilin-A1 BAR domain . J. Mol. Biol. . 351 . 3 . 653–61 . August 2005 . 16023669 . 10.1016/j.jmb.2005.06.013 .
- Gallop JL, Jao CC, Kent HM . Mechanism of endophilin N-BAR domain-mediated membrane curvature . EMBO J. . 25 . 12 . 2898–910 . June 2006 . 16763559 . 1500843 . 10.1038/sj.emboj.7601174. etal.
- Masuda M, Takeda S, Sone M . Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms . EMBO J. . 25 . 12 . 2889–97 . June 2006 . 16763557 . 1500852 . 10.1038/sj.emboj.7601176. etal.
- Frost A, Perera R, Roux A . Structural basis of membrane invagination by F-BAR domains . Cell . 132 . 5 . 807–17 . March 2008 . 18329367 . 2384079 . 10.1016/j.cell.2007.12.041 . etal.
Notes and References
- Web site: Gene group: N-BAR domain containing. HGNC: HUGO gene nomenclature committee.
- Qualmann B, Koch D, Kessels MM . Let's go bananas: revisiting the endocytic BAR code . EMBO J. . 30 . 17 . 3501–15 . August 2011 . 21878992 . 3181480 . 10.1038/emboj.2011.266 .
- Koch D, Spiwoks-Becker I, Sabanov V, Sinning A, Dugladze T, Stellmacher A, Ahuja R, Grimm J, Schüler S, Müller A, Angenstein F, Ahmed T, Diesler A, Moser M, Tom Dieck S, Spessert R, Boeckers TM, Fässler R, Hübner CA, Balschun D, Gloveli T, Kessels MM, Qualmann B . Proper synaptic vesicle formation and neuronal network activity critically rely on syndapin I . EMBO J. . 30 . 24 . 4955–69 . December 2011 . 21926968 . 3243622 . 10.1038/emboj.2011.339 .
