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Blood, Vol. 92 No. 5 (September 1), 1998:
pp. 1697-1706
SLP-76-Cbl-Grb2-Shc Interactions in Fc RI Signaling
Julie Chu,
Yenbou Liu,
Gary A. Koretzky, and
Donald L. Durden
From the Neil Bogart Memorial Laboratories, Division of
Hematology-Oncology, Childrens Hospital Los Angeles, Los Angeles, CA;
University of Southern California School of Medicine, Los Angeles, CA;
and the Departments of Internal Medicine, Physiology, and Biochemistry
and the Graduate Program in Immunology, University of Iowa College of
Medicine, Iowa City, IA.
SLP-76 and Cbl are complex adapter proteins that have the capacity
to bind to smaller adapter proteins, such as Grb2, which subsequently
binds the nucleotide exchange protein Sos in the transmission of
intracellular signals. SLP-76, Cbl, Shc, and Grb2 have been implicated
in immunoreceptor tyrosine-based activation motif (ITAM) signaling,
leading to activation of Ras. However, their mechanism of action has
not been determined. To date, there have been no reports of SLP-76
involvement in Fc RI-receptor signaling and no data exist for an
interaction between Cbl, Shc, and SLP-76 in vivo. We provide evidence
that SLP-76, Cbl, and Shc are tyrosine phosphorylated on
FcRI-receptor stimulation and are associated with the adapter
protein Grb2 in -interferon-differentiated U937 cells (U937IF). The
interactions between SLP-76 and Cbl and SLP-76 and Grb2 are present in
resting U937IF cells. However, the interaction between SLP-76 and Grb2
becomes augmented twofold on FcRI-receptor aggregation. Our results
provide the first evidence for a phosphorylation-dependent interaction
between SLP-76 and Shc, induced at least 10-fold on FcRI receptor
stimulation. Our data indicate that a significant portion of a
multimolecular complex containing Cbl, SLP-76, Shc, and Grb2 is
distinct from a trimolecular complex containing the Ras guanine
nucleotide exchanger Sos, Shc, and Grb2. FcRI-induced tyrosine
phosphorylation of SLP-76, Cbl, Shc, and the highly induced SLP-76-Shc
interaction provide the first evidence that SLP-76 and Cbl are involved
in FcRI signaling and suggest a functional significance for these
interactions in FcRI signal relay in the control of Ras in myeloid
cells.
© 1998 by The American Society of Hematology.
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