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Volume 271, Number 23, Issue of June 7, 1996 pp. 13342-13348
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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A Role for Shc, Grb2, and Raf-1 in FcRI Signal Relay

(Received for publication, November 27, 1995, and in revised form, February 13, 1996)

Rae Kil Park , Yenbou Liu and Donald L. Durden

From the  Neil Bogart Memorial Laboratories, Division of Hematology-Oncology, Childrens Hospital Los Angeles and University of Southern California School of Medicine, Los Angeles, California 90027

The activation of the serine/threonine kinase, Raf-1, serves to connect upstream protein tyrosine kinases to downstream signaling events. We previously reported that FcRI stimulation of interferon -differentiated U937 cells (termed U937IF cells) induces a mobility shift in Erk2. Herein, we report that cross-linking of FcRI receptor in U937IF cells induces a marked tyrosine phosphorylation of Raf-1 (10-fold increase). Tyrosine phosphorylation of Raf-1 is induced by FcRI activation and not by PMA (1 µg/ml), N-formyl-Met-Leu-Phe (1 µM), calcium ionophore (1 µM), thrombin (0.05 unit/ml), FcRII, or FcRIII stimulation. The kinetics of Raf-1 tyrosine phosphorylation is rapid, reaching peak levels 1-2 min after FcRI activation, and the tyrosine phosphorylation of Raf-1 precedes the activation of the respiratory burst. FcRI cross-linking induces the tyrosine phosphorylation of Shc; tyrosine-phosphorylated Shc binds to Grb2 forming a Shc-Grb2 complex. The data provide evidence that the FcRI receptor signals via the upstream activation of nonreceptor protein tyrosine kinases, which leads to the subsequent activation of Ras family GTPases and serine/threonine kinases, Raf-1 and mitogen-activated protein kinase.

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