The Bin/Amphiphysin/Rvs (BAR) domain of the plant SH3 domain-containing proteins
BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. This group is composed of proteins with similarity to Arabidopsis thaliana SH3 domain-containing proteins 1 (SH3P1) and 2 (SH3P2). SH3P1 is involved in the trafficking of clathrin-coated vesicles. It is localized at the plasma membrane and is associated with vesicles of the trans-Golgi network. Yeast complementation studies reveal that SH3P1 has similar functions to the Saccharomyces cerevisiae Rvs167p, which is involved in endocytosis and actin cytoskeletal arrangement. Members of this group contain an N-terminal BAR domain and a C-terminal SH3 domain. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.