regulation of splicing through sam68
| PAG Title | regulation of splicing through sam68 |
| PAG ID | WAG001258 |
| Type | P |
| Source Link |  BioCarta |
| Publication Reference | NA |
| PAG Description | While transcriptiol regulation is often viewed as the most prevalent way extracellular sigls to regulate gene expression, post-transcriptiol regulation of splicing, R stability, and translation are also regulated by extracellular sigls. Sam68, a member of a family of R-binding proteins called STAR proteins, mediates altertive splicing in response to extracellular sigls, such as altered splicing of CD44 in response to phorbol ester treatment of T cells. R binding and activity of SAM68 is regulated by upstream sigls through phosphorylation and modulating of its interaction with other proteins, itself and with R. Phorbol ester treatment of T cells stimulates the ras/ Map kise pathway, activating Erk and phosphorylation of Sam68, inducing altertive splicing of CD44 and perhaps other cellular R targets. Sam68 is localized in the nucleus to a specific substructure called the Sam68/SLM Nuclear Bodies, colocalizing with splicing factors and helping to link perhaps sigl transduction with R processing. Sam68 has been suggested to play a role in a variety of pathways, including insulin sigling and HIV gene expression, substituting for the activity of viral Rev protein, and to be regulated by arginine methylation as well as phosphorylation. In addition to the role of Sam68 regulating posttranscriptiol gene expression, Sam68 also interacts with transcription factors such as CBP and appears to regulate gene expression. |
| Species | Homo sapiens |
| nCoCo Score | 1,301 |
| Base PAG ID | WAG001258 |
| Human Phenotyte Annotation | |
| Curator | PAGER curation team |
| Curator Contact | PAGER-contact@googlegroups.com |
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