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 Previous Article

Mol Cell Biol. 1988 September; 8(9): 3969-3973

Oncogenic activation of p185neu stimulates tyrosine phosphorylation in vivo.

D F Stern, M P Kamps and H Cao

Department of Pathology, Yale University School of Medicine, New Haven, Connecticut 06510.

ABSTRACT

p185, the product of the neu/erbB2 proto-oncogene, is oncogenically activated by a point mutation that substitutes glutamic acid for valine in the transmembrane domain of the protein. We have found that the transforming form of p185 differs from its normal counterpart in inducing increased tyrosine phosphorylation of other proteins in vivo and in having a much shorter half-life. These results support the model that the transforming p185 resembles a ligand-activated receptor.

Mol Cell Biol. 1988 September; 8(9): 3969-3973




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