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J. Biol. Chem., Vol. 269, Issue 40, 24747-24755, 10, 1994
HH Kim, SL Sierke and JG Koland
The ErbB3 protein is a member of the ErbB subfamily of receptor protein
tyrosine kinases. In the present study, the mechanism by which the ErbB3
protein is phosphorylated and the signal-transducing functions of this
phosphorylated protein were investigated. When phosphorylated by the
epidermal growth factor receptor in vitro, the ErbB3 protein strongly
associated with the regulatory p85 subunit and the catalytic activity of
phosphatidylinositol (PI) 3-kinase. The association of PI 3- kinase with
ErbB3 in human breast cancer cells was found to be correlated with the
constitutive phosphorylation of ErbB3 on tyrosine residues. In MDA-MB-468
breast cancer cells in which the ErbB3 protein is not constitutively
phosphorylated, stimulation with epidermal growth factor led to the
phosphorylation of ErbB3 on tyrosine residues and the formation of a
functional signal transduction complex involving the ErbB3 protein and PI
3-kinase. These results suggest that the ErbB3 protein can be
phosphorylated on tyrosine residues by a cross- phosphorylation mechanism
and that the phosphorylated ErbB3 protein can couple other growth factor
receptor protein tyrosine kinases to the PI 3-kinase pathway in a manner
similar to the insulin receptor substrate 1 protein.
Epidermal growth factor-dependent association of phosphatidylinositol 3- kinase with the erbB3 gene product
Department of Pharmacology, University of Iowa, College of Medicine, Iowa City 52242-1109.
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M. Kong, C. Mounier, J. Wu, and B. I. Posner Epidermal Growth Factor-induced Phosphatidylinositol 3-Kinase Activation and DNA Synthesis. IDENTIFICATION OF Grb2-ASSOCIATED BINDER 2 AS THE MAJOR MEDIATOR IN RAT HEPATOCYTES J. Biol. Chem., November 10, 2000; 275(46): 36035 - 36042. [Abstract] [Full Text] [PDF]
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K. Takeuchi, S. Shibamoto, K. Nagamine, I. Shigemori, S. Omura, N. Kitamura, and F. Ito Signaling Pathways Leading to Transcription and Translation Cooperatively Regulate the Transient Increase in Expression of c-Fos Protein J. Biol. Chem., July 6, 2001; 276(28): 26077 - 26083. [Abstract] [Full Text] [PDF]
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S. H. Ong, Y. R. Hadari, N. Gotoh, G. R. Guy, J. Schlessinger, and I. Lax Stimulation of phosphatidylinositol 3-kinase by fibroblast growth factor receptors is mediated by coordinated recruitment of multiple docking proteins PNAS, May 22, 2001; 98(11): 6074 - 6079. [Abstract] [Full Text] [PDF]
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