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

Shahab Uddin, Concetta Gardziola, Aruna Dangat, Taolin Yi, Leonidas C. Platanias*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

30 Scopus citations

Abstract

The c-cbl proto-oncogene product (p120(cbl)) 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, p120(cbl) is rapidly phosphorylated on tyrosine in an IFNα-dependent manner. p120(cbl) 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 p120(cbl) interacts with the functional Type I IFN receptor complex, and suggest its involvement in IFNα signaling.

Original languageEnglish (US)
Pages (from-to)833-838
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume225
Issue number3
DOIs
StatePublished - Aug 23 1996

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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