The BAR (Bin-Amphiphysin-Rvs) domain is about 200 amino acid long. This domain
can be found alone or in association with other domains such as SH3 (see
<PDOC50002>) and RhoGAP (see <PDOC50238>). BAR domain containing proteins are
a unique class of adaptor proteins characterized by a common N-terminal fold
termed the BAR domain. This set of adaptors, which includes the mammalian
proteins amphiphysin and Bin1 and the yeast proteins Rvs167 and Rvs161, has
been implicated in diverse cellular processes, including synaptic vesicle
endocytosis, actin regulation, differentiation, cell survival, and
tumorigenesis. Clearly there are two functions associated with the BAR domain,
the sensing and/or induction of membrane curvature and the binding to a small
The resolution of the N-terminus of amphiphysin has shown that the BAR domain
forms a crescent-shaped dimer of a three-helix coiled-coil with a
characteristic set of conserved hydrophobic, aromatic and hydrophilic amino
acids (see <PDB:1URU>) [3,4]. More structural studies revealed that
dimerization is a minimal function of BAR-domain-containning proteins. It was
suggested that the V-shaped dimer is able to sense and/or induce membrane
More, amphiphysin and endophilin contain a short sequence stretch adjacent to
the N terminus of the BAR domain which is presumed to be essential for
lipid-binding and tubule formation. This sequence at the N-terminal end was
shown to form an amphipathic helix, thereby extending the helical backbone of
the dimer at the tips. Together with the BAR domain, this sequence motif is
termed N-BAR and can be found in a subgroup of the BAR-domain family including
amphiphysin. This stretch is not covered by the developed profile.
Some proteins known to contain a BAR domain are listed below:
The profile we developed covers the entire BAR domain.
This profile picks up the entire Bin-Amphiphysin-Rvs family. But recent
papers, based on sequence and structural similarities have shown that a
conserved region in more divergent families, like oligophrenin, centaurin
β, sorting nexin, ICA69, pick1 or arfaptins, is related to the BAR domain
[6,7,8]. These families are however too divergent to be detected by this
September 2004 / First entry.
PROSITE method (with tools and information) covered by this documentation:
Balguerie A. Sivadon P. Bonneu M. Aigle M.
Rvs167p, the budding yeast homolog of amphiphysin, colocalizes with actin patches.
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