| First Author | Gu H | Year | 1998 |
| Journal | Mol Cell | Volume | 2 |
| Issue | 6 | Pages | 729-40 |
| PubMed ID | 9885561 | Mgi Jnum | J:51807 |
| Mgi Id | MGI:1326955 | Doi | 10.1016/s1097-2765(00)80288-9 |
| Citation | Gu H, et al. (1998) Cloning of p97/Gab2, the major SHP2-binding protein in hematopoietic cells, reveals a novel pathway for cytokine-induced gene activation. Mol Cell 2(6):729-40 |
| abstractText | Several components in cytokine signaling remain unidentified. We report the cloning and initial characterization of one such component, p97, a widely expressed scaffolding protein distantly related to Drosophila DOS and mammalian Gab1. Upon cytokine, growth factor, or antigen receptor stimulation, p97 becomes tyrosyl phosphorylated and associates with several SH2 domain-containing proteins, including SHP2. Expression of p97 mutants unable to bind SHP2 blocks cytokine-induced c-fos promoter activation, inhibiting Elk1-mediated and STAT5-mediated transactivation. Surprisingly, such mutants do not inhibit MAPK activation. Our results identify p97 as an important regulator of receptor signaling that controls a novel pathway to immediate-early gene activation and suggest multiple functions for SHP2 in cytokine receptor signaling. |
