Interaction of p59(fyn) with interferon-activated Jak kinases

Shahab Uddin, Dorie A. Sher, Yazan Alsayed, Sebastian Pons, Oscar R. Colamonici, Eleanor N. Fish, Morris F. White, Leonidas C. Platanias*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

44 Scopus citations

Abstract

During IFNα stimulation, p59(fyn) associates with the Type I IFNR-associated Tyk-2 kinase in several human hematopoietic cell lines in vivo. This interaction is direct, and is mediated by the SH2 domain in p59(fyn), as shown by binding studies using glutathione-S-tranferase fusion proteins and far western blots. Furthermore, in response to IFNα-treatment of cells, the SH2 domain of Fyn interacts with the Tyk-2-associated c-cbl proto-oncogene product. In a similar manner, during IFNγ stimulation, p59(fyn) associates via its SH2 domain with the activated form of the IFNγ-dependent Jak-2 kinase. These data suggest that p59(fyn) is a common element in IFNα and IFNγ signaling, and is selectively engaged by the Type I or II IFN receptors via specific interactions with dis-tinct Jak kinases.

Original languageEnglish (US)
Pages (from-to)83-88
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume235
Issue number1
DOIs
StatePublished - Jun 9 1997

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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