Activation of a CrkL-Stat5 signaling complex by type I interferons

Eleanor N. Fish, Shahab Uddin, Mete Korkmaz, Beata Majchrzak, Brian J. Druker, Leonidas C. Platanias

Research output: Contribution to journalArticlepeer-review

124 Scopus citations


Type I interferons (IFNα and IFNβ) 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 IFNα 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.

Original languageEnglish (US)
Pages (from-to)571-573
Number of pages3
JournalJournal of Biological Chemistry
Issue number2
StatePublished - Jan 8 1999

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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