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BAR domain

Class: Phospholipid Binding

Brief description: BAR (Bin/Amphiphysin/Rvs) domains are highly conserved protein dimerization domains that occur in many proteins. Thye are approxmately 250 amino acids long and are involved in a lot of functions such as muscle T cell tubule formation, synaptic vesicle endosytosis and membrane remodeling. They have been proposed to bend and tubulate vesicles in vitro. It has also been proposed that they are capable of sensing membrane curvature by binding preferentially to curved membranes. Some BAR domains also have SH3 domains that bind to dynamin and thus proteins like amphiphysin and endophilin are implicated in the orchestration of vesicle scission.

Structure:

structure The BAR domain is banana shaped dimer; each monomber is made of a coiled-coil of three long alpha-helices. The concave surface of the dimer interacts with the anionic membrane lipids (primarily through electrostatic interactions) via several cationic residues. Owing to the rigid concave shape of their binding surface, they can either bend the membranes or simply sense the curved membranes. BAR domains have an N-terminal extension like an amphiphilic a-helix upon binding which is important but not essential for vesicle tubulation.

Subcellular Localization:

BAR-domain-containing proteins have been shown to bind to lipids and to bend membranes. Amphiphysins and Endophilins, the first such proteins to be discovered, respectively form clathrin-coated vesicles and induce membrane curvature. Several proteins that have been predicted to have a BAR domain have been shown to interact with small GTPases. The BAR domain of the Arfaptins was shown to bind to the small GTPases Rac, Arf1, Arf3 and Arf6, as well as to Arl1.

Get the sequences in a Swiss-Prot/Uniprot pattern and Tab-delimited format.

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Relevant Literature

1. Peter, B.J., Kent, H.M., Mills, I.G., Vallis, Y., Butler, P.J., Evans, P.R. and McMahon, H.T. (2004) BAR domains as sensors of membrane curvature: the amphiphysin BAR structure. Science, 303, 495-499.

2. Habermann, B. (2004) The BAR-domain family of proteins: a case of bending and binding? EMBO Rep, 5, 250-255.

3. Ge, K. and Prendergast, G.C. (2000) Bin2, a functionally nonredundant member of the BAR adaptor gene family. Genomics, 67, 210-220.

4. Weissenhorn, W. (2005) Crystal structure of the endophilin-A1 BAR domain. J Mol Biol, 351, 653-661.