Glycogen Synthase Kinase-3β Facilitates IFN-γ-Induced STAT1 Activation by Regulating Src Homology-2 Domain-Containing Phosphatase 2
作者： Cheng-Chieh Tsai , Jui-In Kai , Wei-Ching Huang , Chi-Yun Wang , Yi Wang
关键词: GSK-3 、 Proto-oncogene tyrosine-protein kinase Src 、 Phospholipase A 、 Glycogen synthase 、 Biochemistry 、 Phosphorylation 、 Biology 、 Phosphatase 、 Protein kinase C 、 Cell biology 、 Phospholipase C
摘要: Glycogen synthase kinase-3β (GSK-3β)-modulated IFN-γ-induced inflammation has been reported; however, the mechanism that activates GSK-3β and effects of activation remain unclear. Inhibiting decreased inflammation. IFN-γ treatment rapidly activated via neutral sphingomyelinase- okadaic acid-sensitive phosphatase-regulated dephosphorylation at Ser 9 , proline-rich tyrosine kinase 2 (Pyk2)-regulated phosphorylation Tyr 216 . Pyk2 was through phosphatidylcholine-specific phospholipase C (PC-PLC)-, protein (PKC)-, Src-regulated pathways. The PC-PLC, Pyk2, potentially regulated by receptor 2-associated Jak2, but it independent 1. Furthermore, Jak2/PC-PLC/PKC/cytosolic A positively sphingomyelinase. Src homology-2 domain-containing phosphatase (SHP2), thereby preventing STAT1 in late stage stimulation. All these results showed synergistically affected inhibiting SHP2.
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