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Specific inhibition of Stat3 signal transduction by PIAS3 总被引:1,自引:0,他引:1
CD Chung J Liao B Liu X Rao P Jay P Berta K Shuai 《Canadian Metallurgical Quarterly》1997,278(5344):1803-1805
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T Bellido CA O'Brien PK Roberson SC Manolagas 《Canadian Metallurgical Quarterly》1998,273(33):21137-21144
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M Wartmann N Cella P Hofer B Groner X Liu L Hennighausen NE Hynes 《Canadian Metallurgical Quarterly》1996,271(50):31863-31868
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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. 相似文献
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