| Primary Identifier | IPR003023 | Type | Family |
| Short Name | Amphiphysin_2 |
| description | Amphiphysins belong to the expanding BAR (Bin-Amphiphysin-Rvsp) family proteins, all members of which share a highly conserved N-terminal BAR domain, which has predicted coiled-coil structures required for amphiphysin dimerisation and plasma membrane interaction []. Almost all members also share a conserved C-terminal Src homology 3 (SH3) domain, which mediates their interactions with the GTPase dynamin and the inositol-5'-phosphatase synaptojanin 1 in vertebrates and with actin in yeast. The central region of all these proteins is most variable. In mammals, the central region of amphiphysin I and amphiphysin IIa contains a proline-arginine-rich region for endophilin binding and a CLAP domain, for binding to clathrin and AP-2. The interactions mediated by both the central and C-terminal domains arebelieved to be modulated by protein phosphorylation [, ].Amphiphysins are proteins that are thought to be involved in clathrin-mediated endocytosis, actin function, and signalling pathways. In vertebrates, amphiphysins may regulate, but are not essential for clathrin-mediated endocytosis of SVs. However, in Drosophila amphiphysin is not involved at all in SV endocytosis but is required for T-tubule structure and excitation-contraction coupling muscles and plays a role in membrane morphogenesis in developing photoreceptors and a variety of other cells [].Amphiphysin 2 was the second amphiphysin family member found in mammals.The gene encoding it has been found to be alternatively spliced. Thevarious products have been named: BIN-1, Sh3P9, BRAMP-2 and ALP-1. Theyhave different distribution patterns, with the largest form (~95 kD) beingexpressed solely in the brain, where it shares a very similar (if notidentical) distribution pattern to amphiphysin 1 []. |
