| Literature DB >> 7629131 |
A Yetter1, S Uddin, J J Krolewski, H Jiao, T Yi, L C Platanias.
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.Entities:
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Year: 1995 PMID: 7629131 DOI: 10.1074/jbc.270.31.18179
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157