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J Biol Chem, Vol. 273, Issue 33, 21239-21245, August 14, 1998
From the Department of Physiology, University of Michigan Medical
School, Ann Arbor, Michigan 48109-0622
We recently identified SH2-B
Platelet-derived Growth Factor (PDGF) Stimulates the Association
of SH2-B
with PDGF Receptor and Phosphorylation of SH2-B
as a JAK2-binding
protein and substrate involved in the signaling of receptors for growth
hormone and interferon-
. In this work, we report that SH2-B also
functions as a signaling molecule for platelet-derived growth factor
(PDGF). SH2-B fused to glutathione S-transferase (GST)
bound PDGF receptor (PDGFR) from PDGF-treated but not control cells.
GST fusion protein containing only the SH2 domain of SH2-B also
bound PDGFR from PDGF-treated cells. An Arg to Glu mutation within the
FLVRQS motif in the SH2 domain of SH2-B inhibited GST-SH2-B
binding to tyrosyl-phosphorylated PDGFR. The N-terminal truncated
SH2-B containing the entire SH2 domain interacted directly with
tyrosyl-phosphorylated PDGFR from PDGF-treated cells but not
unphosphorylated PDGFR from control cells in a Far Western assay. These
results suggest that the SH2 domain of SH2-B is necessary and
sufficient to mediate the interaction between SH2-B and PDGFR. PDGF
stimulated coimmunoprecipitation of endogenous SH2-B with endogenous
PDGFR in both 3T3-F442A and NIH3T3 cells. PDGF stimulated the rapid and
transient phosphorylation of SH2-B on tyrosines and most likely on
serines and/or threonines. Similarly, epidermal growth factor
stimulated the phosphorylation of SH2-B; however, phosphorylation
appears to be predominantly on serines and/or threonines. In response
to PDGF, SH2-B associated with multiple tyrosyl-phosphorylated
proteins, at least one of which (designated p84) does not bind to
PDGFR. Taken together, these data strongly argue that, in response to
PDGF, SH2-B directly interacts with PDGFR and is phosphorylated on
tyrosine and most likely on serines and/or threonines, and acts as a
signaling protein for PDGFR.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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