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J Biol Chem, Vol. 274, Issue 2, 571-573, January 8, 1999
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From the Type I interferons (IFN Department of Medical Genetics and
Microbiology, University of Toronto, Toronto, Ontario M5S 3E2, Canada,
the § Section of Hematology-Oncology, University of Illinois
and West Side Veterans Affairs Hospital, Chicago, Illinois 60607, and
the ¶ Division of Hematology and Medical Oncology, Oregon Health
Sciences University, Portland, Oregon 97201
and IFN
) transduce
signals by inducing tyrosine phosphorylation of Jaks and Stats, as well
as the CrkL adapter, an SH2/SH3-containing protein which provides a
link to downstream pathways that mediate growth inhibition. We report that Stat5 interacts constitutively with the IFN receptor-associated Tyk-2 kinase, and during IFN stimulation its tyrosine-phosphorylated form acts as a docking site for the SH2 domain of CrkL. CrkL and Stat5
then form a complex that translocates to the nucleus. This IFN-inducible CrkL-Stat5 complex binds in vitro to the
TTCTAGGAA palindromic element found in the promoters of a subset of
IFN-stimulated genes. Thus, during activation of the Type I IFN
receptor, CrkL functions as a nuclear adapter protein and, in
association with Stat5, regulates gene transcription through DNA binding.
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