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  • Title: Association of the interferon-dependent tyrosine kinase Tyk-2 with the hematopoietic cell phosphatase.
    Author: Yetter A, Uddin S, Krolewski JJ, Jiao H, Yi T, Platanias LC.
    Journal: J Biol Chem; 1995 Aug 04; 270(31):18179-82. PubMed ID: 7629131.
    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.
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