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J Biol Chem, Vol. 273, Issue 27, 16643-16646, July 3, 1998
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From the The ErbB family of receptors, which include the
epidermal growth factor receptor (EGFR), ErbB2, ErbB3, and ErbB4
mediate the actions of a family of bioactive polypeptides. EGF signals
through EGFR, whereas heregulin (HRG) signaling is initiated through
binding to either ErbB3 or ErbB4. In this report we studied the role of protein-tyrosine phosphatase SHP-2 in ErbB-mediated activation of
mitogen-activated protein kinase (MAPK) by overexpressing SHP-2 mutants
in COS-7 cells. We demonstrate that enzymatic activity and both
NH2- and COOH-terminal SH2 domains of SHP-2 are
required for EGF-induced MAPK activation, but not for c-Jun
amino-terminal kinase stimulation or MAPK activation which occurred in
response to myristoylated son of sevenless, activated Ras, or phorbol
ester. Dominant-negative forms of SHP-2 had no effect on EGF-stimulated interaction of GRB2 with EGFR or SHC, nor did they influence
phosphorylation of SHC and SHC/EGFR association. The same mutant SHP-2
structures that inhibited EGF-mediated stimulation of MAPK also blocked
HRG Division of Cytokine Biology, Center for
Biologics Evaluation and Research, Food and Drug Administration,
Bethesda, Maryland 20892, the § Laboratory of Tumor
Immunology and Biology, NCI, National Institutes of Health, Bethesda,
Maryland 20892, the ¶ Department of Biological Chemistry,
University of Michigan Medical School, Ann Arbor, Michigan 48109, the
Oral and Pharyngeal Cancer Branch, NIDR, National Institutes of
Health, Bethesda, Maryland 20892, and the ** Department of Protein
Chemistry and Biophysics, Berlex Biosciences, Richmond, California
94804
/
-induced MAPK activation. EGF or HRG caused SHP-2 SH2
domains to engage multiple phosphotyrosine proteins, and mutation of
either domain disrupted these associations. These results demonstrate that SHP-2 performs a common and essential function(s) in
ligand-stimulated MAPK activation by the ErbB family of receptors.
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