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	J. Biol. Chem. Aug (1995); 270(31):18179-82
Association of the interferon-dependent tyrosine kinase Tyk-2 with the hematopoietic cell phosphatase.
Yetter A, Uddin S, Krolewski JJ, Jiao H, Yi T, Platanias LC
Division of Hematology-Oncology, Loyola University of Chicago, Maywood, Illinois 60153, USA.
Abstract: The tyrosine kinase Tyk-2 is physically associated with the Type I interferon (IFN) receptor complex and is rapidly activated during IFN alpha stimulation. We report that Tyk-2 forms stable complexes with the SH2-containing hematopoietic cell phosphatase (HCP) in several hematopoietic cell lines in vivo, and that the IFN alpha-induced tyrosine-phosphorylated form of Tyk-2 is a substrate for the phosphatase activity of HCP in in vitro assays. Furthermore, treatment of cells with the phosphatase inhibitor sodium orthovanadate induces tyrosine phosphorylation of Tyk-2 and an associated 115-kDa protein. Altogether, these data suggest that HCP regulates tyrosine phosphorylation of the Tyk-2 kinase, and thus its function may be important in the transmission of signals generated at the Type I IFN receptor level.
[PUBMED: 7629131]