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Volume 272, Number 48, Issue of November 28, 1997 pp. 29991-29994
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

COMMUNICATION:
The Type I Interferon Receptor Mediates Tyrosine Phosphorylation of the CrkL Adaptor Protein

(Received for publication, September 9, 1997)

Sarfraz Ahmad , Yazan M. Alsayed , Brian J. Druker ^§ and Leonidas C. Platanias

From the  Section of Hematology-Oncology, University of Illinois at Chicago and West Side Veterans Administration Hospital, Chicago, Illinois 60607 and the ^§ Division of Hematology and Medical Oncology, Oregon Health Sciences University, Portland, Oregon 97201

Interferon (IFN)  induces rapid and transient tyrosine phosphorylation of the Src homology 2/Src homology 3 (SH2/SH3)-containing CrkL adaptor protein in a time- and dose-dependent manner. Such phosphorylation is most likely regulated by the Type I interferon receptor (IFNR)-associated Tyk-2 kinase, as suggested by the detection of Type I IFN-dependent tyrosine kinase activity in anti-CrkL immunoprecipitates and the IFN-dependent association of CrkL with Tyk-2 in intact cells. Two other Type I IFNs, IFN and IFN, also induce tyrosine phosphorylation of CrkL, suggesting that the protein is involved in the signaling pathways of several different Type I IFNs. In the IFN-sensitive U-266 and Daudi cell lines, CrkL interacts via its N terminus SH3 domain with the guanine exchange factor C3G that regulates activation of Rap-1, a small G-protein that exhibits tumor suppressor activity. Thus, tyrosine phosphorylation of CrkL links the functional Type I IFNR complex to the C3G-Rap-1 signaling cascade that mediates growth inhibitory responses.

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