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Biochem Biophys Res Commun. 1996 Aug 23;225(3):833-8.

Interaction of the c-cbl proto-oncogene product with the Tyk-2 protein tyrosine kinase.

Author information

1
Division of Hematology-Oncology, Loyola University Chicago, Maywood, Illinois 60153, USA.

Abstract

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.

PMID:
8780698
DOI:
10.1006/bbrc.1996.1259
[Indexed for MEDLINE]

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