BAR domain

BAR (Bin–Amphiphysin–Rvs) 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. The occurrence in different protein and more information can be found on endocytosis.org.

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.

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 remains to be elucidated. Syndapin/pacsin proteins are an example of an F-BAR protein family.

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;

Publications

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