BAR domain

BAR domain
Structure of amphiphysin BAR.
Identifiers
SymbolBAR
PfamPF03114
InterProIPR004148
SMARTSM00721
PROSITEPDOC51021
SCOP21uru / SCOPe / SUPFAM
CDDcd07307
Available protein structures:
PDB  IPR004148 PF03114 (ECOD; PDBsum)  
AlphaFold
Bin/amphiphysin/Rvs domain
Identifiers
SymbolBAR-2
PfamPF10455
Available protein structures:
PDB  PF10455 (ECOD; PDBsum)  
AlphaFold
BAR domain of APPL family
Identifiers
SymbolBAR-3
PfamPF16746
Available protein structures:
PDB  PF16746 (ECOD; PDBsum)  
AlphaFold
EFC/F-BAR homology domain
Identifiers
SymbolFCH
PfamPF00611
Available protein structures:
PDB  PF00611 (ECOD; PDBsum)  
AlphaFold
Vps5 C terminal like (BAR domain)
Identifiers
SymbolVps5
PfamPF09325
InterProIPR015404
Available protein structures:
PDB  IPR015404 PF09325 (ECOD; PDBsum)  
AlphaFold
WASP-binding domain of sorting nexin proteins
Identifiers
SymbolBAR-3-WASP
PfamPF10456
Available protein structures:
PDB  PF10456 (ECOD; PDBsum)  
AlphaFold

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

References

  1. 1 2 Peter BJ, Kent HM, Mills IG, Vallis Y, Butler PJ, Evans PR, et al. (January 2004). "BAR domains as sensors of membrane curvature: the amphiphysin BAR structure". Science. 303 (5657). New York, N.Y.: 495–499. doi:10.1126/science.1092586. PMID 14645856.
  2. ↑ Gallop JL, Jao CC, Kent HM, Butler PJ, Evans PR, Langen R, et al. (June 2006). "Mechanism of endophilin N-BAR domain-mediated membrane curvature". The EMBO Journal. 25 (12): 2898–2910. doi:10.1038/sj.emboj.7601174. PMC 1500843. PMID 16763559.
  3. ↑ Masuda M, Takeda S, Sone M, Ohki T, Mori H, Kamioka Y, et al. (June 2006). "Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms". The EMBO Journal. 25 (12): 2889–2897. doi:10.1038/sj.emboj.7601176. PMC 1500852. PMID 16763557.
  4. ↑ Weissenhorn W (August 2005). "Crystal structure of the endophilin-A1 BAR domain". Journal of Molecular Biology. 351 (3): 653–661. doi:10.1016/j.jmb.2005.06.013. PMID 16023669.
  5. ↑ Itoh T, Erdmann KS, Roux A, Habermann B, Werner H, De Camilli P (December 2005). "Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins". Developmental Cell. 9 (6): 791–804. doi:10.1016/j.devcel.2005.11.005. PMID 16326391.
  6. ↑ Tsujita K, Suetsugu S, Sasaki N, Furutani M, Oikawa T, Takenawa T (January 2006). "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. doi:10.1083/jcb.200508091. PMC 2063556. PMID 16418535.
  7. ↑ Shimada A, Niwa H, Tsujita K, Suetsugu S, Nitta K, Hanawa-Suetsugu K, et al. (May 2007). "Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis". Cell. 129 (4): 761–772. doi:10.1016/j.cell.2007.03.040. PMID 17512409.
  8. ↑ Qualmann B, Koch D, Kessels MM (August 2011). "Let's go bananas: revisiting the endocytic BAR code". The EMBO Journal. 30 (17): 3501–3515. doi:10.1038/emboj.2011.266. PMC 3181480. PMID 21878992.
  9. ↑ Koch D, Spiwoks-Becker I, Sabanov V, Sinning A, Dugladze T, Stellmacher A, et al. (December 2011). "Proper synaptic vesicle formation and neuronal network activity critically rely on syndapin I". The EMBO Journal. 30 (24): 4955–4969. doi:10.1038/emboj.2011.339. PMC 3243622. PMID 21926968.
  10. ↑ "Gene group: N-BAR domain containing". HGNC: HUGO gene nomenclature committee.

Further reading

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