BAR domain
Structure of amphiphysin BAR.[1]
Identifiers
SymbolBAR
PfamPF03114
InterProIPR004148
SMARTSM00721
PROSITEPDOC51021
SCOP21uru / SCOPe / SUPFAM
CDDcd07307
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Bin/amphiphysin/Rvs domain
Identifiers
SymbolBAR-2
PfamPF10455
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
BAR domain of APPL family
Identifiers
SymbolBAR-3
PfamPF16746
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
EFC/F-BAR homology domain
Identifiers
SymbolFCH
PfamPF00611
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Vps5 C terminal like (BAR domain)
Identifiers
SymbolVps5
PfamPF09325
InterProIPR015404
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
WASP-binding domain of sorting nexin proteins
Identifiers
SymbolBAR-3-WASP
PfamPF10456
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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.[1]

Human proteins containing this domain

AMPH; ARHGAP17; ARHGAP44; BIN1; BIN2; BIN3; SH3BP1; SH3GL1; SH3GL2; SH3GL3; SH3GLB1; SH3GLB2.[2]

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.[3] 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.[4]

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

References

  1. 1 2 Peter BJ, Kent HM, Mills IG, et al. (January 2004). "BAR domains as sensors of membrane curvature: the amphiphysin BAR structure". Science. 303 (5657): 495–9. doi:10.1126/science.1092586. PMID 14645856. S2CID 6104655.
  2. "Gene group: N-BAR domain containing". HGNC: HUGO gene nomenclature committee.
  3. Qualmann B, Koch D, Kessels MM (August 2011). "Let's go bananas: revisiting the endocytic BAR code". EMBO J. 30 (17): 3501–15. doi:10.1038/emboj.2011.266. PMC 3181480. PMID 21878992.
  4. 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 (December 2011). "Proper synaptic vesicle formation and neuronal network activity critically rely on syndapin I". EMBO J. 30 (24): 4955–69. doi:10.1038/emboj.2011.339. PMC 3243622. PMID 21926968.

Further reading

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