Uddin S, Gardziola C, Dangat A, Yi T, Platanias L C
Division of Hematology-Oncology, Loyola University Chicago, Maywood, Illinois 60153, USA.
Biochem Biophys Res Commun. 1996 Aug 23;225(3):833-8. doi: 10.1006/bbrc.1996.1259.
The c-cbl proto-oncogene product (p120cbl) forms a stable complex with the Tyk-2 protein tyrosine kinase in various human cell lines of diverse hematopoietic origin. In U-266 myeloma and 293T embryonic kidney cells, p120cbl is rapidly phosphorylated on tyrosine in an IFN alpha-dependent manner. p120cbl also acts as a specific substrate for the Tyk-2-associated SHP-1 phosphatase in vitro, suggesting that this phosphatase plays a regulatory role on the phosphorylation of the protein. These data provide evidence that p120cbl interacts with the functional Type I IFN receptor complex, and suggest its involvement in IFN alpha signaling.
原癌基因c-cbl产物（p120cbl）在多种造血来源的人类细胞系中与Tyk-2蛋白酪氨酸激酶形成稳定复合物。在U-266骨髓瘤细胞和293T胚胎肾细胞中，p120cbl以IFNα依赖的方式在酪氨酸位点快速磷酸化。在体外，p120cbl还是与Tyk-2相关的SHP-1磷酸酶的特异性底物，表明该磷酸酶对该蛋白的磷酸化起调节作用。这些数据证明p120cbl与功能性I型干扰素受体复合物相互作用，并提示其参与IFNα信号传导。
