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J Biol Chem, Vol. 273, Issue 33, 20996-21002, August 14, 1998
From the Department of Pharmacology, the University of Iowa College
of Medicine, Iowa City, Iowa 52242-1109
The ErbB2 and ErbB3 proteins together constitute
a functional coreceptor for heregulin (neuregulin). Heregulin
stimulates the phosphorylation of both coreceptor constituents and
initiates a variety of other signaling events, which include
phosphorylation of the Shc protein. The role of Shc in
heregulin-stimulated signal transduction through the ErbB2·ErbB3
coreceptor was investigated here. Heregulin was found to promote
ErbB3/Shc association in NIH-3T3 cells expressing endogenous ErbB2 and
recombinant ErbB3. A mutant ErbB3 protein was generated in which
Tyr-1325 in a consensus Shc phosphotyrosine-binding domain recognition
site was mutated to Phe (ErbB3-Y/F). This mutation abolished the
association of Shc with ErbB3 and blocked the activation of
mitogen-activated protein kinase by heregulin. Whereas heregulin
induced mitogenesis in NIH-3T3 cells transfected with wild-type ErbB3
cDNA, this mitogenic response was markedly attenuated in NIH-3T3
cells transfected with the ErbB3-Y/F cDNA. These results showed a
specific interaction of Shc with the ErbB3 receptor protein and
demonstrated the importance of this interaction in the activation of
mitogenic responses by the ErbB2·ErbB3 heregulin coreceptor
complex.
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