| First Author | Alvarez CE | Year | 2002 |
| Journal | J Biol Chem | Volume | 277 |
| Issue | 27 | Pages | 24728-34 |
| PubMed ID | 12006592 | Mgi Jnum | J:77773 |
| Mgi Id | MGI:2182538 | Doi | 10.1074/jbc.M202512200 |
| Citation | Alvarez CE, et al. (2002) Novel Isoform of Insulin Receptor Substrate p53/p58 Is Generated by Alternative Splicing in the CRIB/SH3-binding Region. J Biol Chem 277(27):24728-34 |
| abstractText | Insulin receptor substrate p53/p58 (IRSp53) is involved in cytoskeletal dynamics and is a candidate disease sensor in polyglutamine expansion neurodegeneration. It is widely expressed throughout the body, but its levels are dramatically elevated in forebrain regions. IRSp53 functions as a signal transducing adaptor between activated Rho family GTPases and their effectors. There are four known alternatively spliced isoforms of IRSp53 that vary by the identity of the 3'-terminal exon. We report here that there is a fifth alternatively spliced isoform, IRSp53-B, which lacks 40 amino acids abutting the CRIB/SH3 (Cdc42/Rac-interactive binding/Src homology 3)-binding site. We speculate that the novel form has an altered function related to the mechanism of autoinactivation. IRSp53-B has an odd history in the mammalian lineage, which may complicate the use of rodent models to study cytoskeletal reorganization. |
