Biology:BAR domain
| BAR domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Structure of amphiphysin BAR. | |||||||||
| Identifiers | |||||||||
| Symbol | BAR | ||||||||
| Pfam | PF03114 | ||||||||
| InterPro | IPR004148 | ||||||||
| SMART | SM00721 | ||||||||
| PROSITE | PDOC51021 | ||||||||
| SCOP2 | 1uru / SCOPe / SUPFAM | ||||||||
| CDD | cd07307 | ||||||||
| |||||||||
| Bin/amphiphysin/Rvs domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | BAR-2 | ||||||||
| Pfam | PF10455 | ||||||||
| |||||||||
| BAR domain of APPL family | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | BAR-3 | ||||||||
| Pfam | PF16746 | ||||||||
| |||||||||
| EFC/F-BAR homology domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | FCH | ||||||||
| Pfam | PF00611 | ||||||||
| |||||||||
| Vps5 C terminal like (BAR domain) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Vps5 | ||||||||
| Pfam | PF09325 | ||||||||
| InterPro | IPR015404 | ||||||||
| |||||||||
| WASP-binding domain of sorting nexin proteins | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | BAR-3-WASP | ||||||||
| 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.
Occurrence 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 WASP family proteins and thus proteins like amphiphysin and endophilin are implicated in the orchestration of vesicle scission and actin cytoskeletal remodeling.
N-BAR domain
Some BAR domain containing proteins have an N-terminal amphipathic helix preceding the BAR domain.[1] This helix inserts (like in the epsin ENTH domain) into the membrane and induces curvature, which is stabilised by the BAR dimer. Amphiphysin, endophilin,[2][3][4] BRAP1/bin2 and nadrin are examples of such proteins containing an N-BAR[1]. The Drosophila amphiphysin N-BAR (DA-N-BAR) is an example of a protein with a preference for negatively charged surfaces.
F-BAR (EFC) domain
Examples of the F-BAR domain family are CIP4/FBP17/Toca-1, Syndapins (also called PACSINs) and muniscins.[5] or EFC for Extended FCH Homology[6]) 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.[7][8]
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.[9]
Human proteins containing this domain
AMPH; ARHGAP17; ARHGAP44; BIN1; BIN2; BIN3; SH3BP1; SH3GL1; SH3GL2; SH3GL3; SH3GLB1; SH3GLB2.[10]
The sorting nexin family of proteins includes several members that possess a BAR domain, including the well characterized SNX1 and SNX9.
See also
- Arfaptin, includes a BAR-like domain
- I-BAR/IMD domain, a BAR-like domain with inverse curvature
- SNX8 - protein family with a combination of BAR-like and PX domains
- Epsin
- Membrane curvature
External links
References
- ↑ 1.0 1.1 "BAR domains as sensors of membrane curvature: the amphiphysin BAR structure". Science (New York, N.Y.) 303 (5657): 495–499. January 2004. doi:10.1126/science.1092586. PMID 14645856.
- ↑ "Mechanism of endophilin N-BAR domain-mediated membrane curvature". The EMBO Journal 25 (12): 2898–2910. June 2006. doi:10.1038/sj.emboj.7601174. PMID 16763559.
- ↑ "Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms". The EMBO Journal 25 (12): 2889–2897. June 2006. doi:10.1038/sj.emboj.7601176. PMID 16763557.
- ↑ "Crystal structure of the endophilin-A1 BAR domain". Journal of Molecular Biology 351 (3): 653–661. August 2005. doi:10.1016/j.jmb.2005.06.013. PMID 16023669.
- ↑ "Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins". Developmental Cell 9 (6): 791–804. December 2005. doi:10.1016/j.devcel.2005.11.005. PMID 16326391.
- ↑ "Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis". The Journal of Cell Biology 172 (2): 269–279. January 2006. doi:10.1083/jcb.200508091. PMID 16418535.
- ↑ "Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis". Cell 129 (4): 761–772. May 2007. doi:10.1016/j.cell.2007.03.040. PMID 17512409.
- ↑ "Let's go bananas: revisiting the endocytic BAR code". The EMBO Journal 30 (17): 3501–3515. August 2011. doi:10.1038/emboj.2011.266. PMID 21878992.
- ↑ "Proper synaptic vesicle formation and neuronal network activity critically rely on syndapin I". The EMBO Journal 30 (24): 4955–4969. December 2011. doi:10.1038/emboj.2011.339. PMID 21926968.
- ↑ "Gene group: N-BAR domain containing". HGNC: HUGO gene nomenclature committee. https://www.genenames.org/data/genegroup/#!/group/1289.
Further reading
- "Drosophila Amphiphysin is a post-synaptic protein required for normal locomotion but not endocytosis". Traffic (Copenhagen, Denmark) 2 (11): 839–850. November 2001. doi:10.1034/j.1600-0854.2001.21113.x. PMID 11733051.
- "Amphiphysins: raising the BAR for synaptic vesicle recycling and membrane dynamics. Bin-Amphiphysin-Rvsp". Traffic (Copenhagen, Denmark) 3 (7): 452–460. July 2002. doi:10.1034/j.1600-0854.2002.30702.x. PMID 12047553.Review.
- "Drosophila Amphiphysin is implicated in protein localization and membrane morphogenesis but not in synaptic vesicle endocytosis". Development (Cambridge, England) 128 (24): 5005–5015. December 2001. doi:10.1242/dev.128.24.5005. PMID 11748137.
- "Drosophila amphiphysin functions during synaptic Fasciclin II membrane cycling". The Journal of Neuroscience 23 (33): 10710–10716. November 2003. doi:10.1523/JNEUROSCI.23-33-10710.2003. PMID 14627656.
- "Structural basis of membrane invagination by F-BAR domains". Cell 132 (5): 807–817. March 2008. doi:10.1016/j.cell.2007.12.041. PMID 18329367.
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