| First Author | Leprince C | Year | 1997 |
| Journal | J Biol Chem | Volume | 272 |
| Issue | 24 | Pages | 15101-5 |
| PubMed ID | 9182529 | Mgi Jnum | J:41089 |
| Mgi Id | MGI:892832 | Doi | 10.1074/jbc.272.24.15101 |
| Citation | Leprince C, et al. (1997) A new member of the amphiphysin family connecting endocytosis and signal transduction pathways. J Biol Chem 272(24):15101-5 |
| abstractText | Src homology 3 (SH3) domains are conserved modules which participate in protein interaction by recognizing proline-rich motifs on target molecules. To identify new SH3-containing proteins, we performed a two-hybrid screen with a proline-rich region of human SOS-1. One of the specific SOS-1 interacting clones that were isolated from a mouse brain cDNA library defines a new protein that was named amphiphysin 2 because of its homology to the previously reported amphiphysin. Amphiphysin 2 is expressed in a number of mouse tissues through multiple RNA transcripts. Here, we report the amino acid sequence of a brain form of amphiphysin 2 (BRAMP2) encoded by a 2. 5-kilobase mRNA. BRAMP2 associates in vitro with elements of the endocytosis machinery such as alpha-adaptin and dynamin. On a biosensor surface, the BRAMP2/dynamin interaction appeared to be direct and partly dependent on a proline-rich sequence of dynamin. Association with dynamin was also observed in PC12 cells after cell stimulation with nerve growth factor, suggesting that amphiphysin 2 may be connected to receptor-dependent signaling pathways. This hypothesis is strengthened by the ability of BRAMP2 to interact with the p21(ras) exchange factor SOS, in vitro, as a possible point of interconnection between the endocytic and signaling pathways. |
