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J. Virol., Jun 1995, 3631-3638, Vol 69, No. 6
Copyright © 1995, American Society for Microbiology

Tissue- and transformation-specific phosphotyrosyl proteins in v-erbB- transformed cells

MJ McManus, DC Connolly and NJ Maihle
Department of Pediatric and Adolescent Medicine, Mayo Foundation, Rochester, Minnesota 55905, USA.

To understand the mechanism of tissue-specific and transformation- specific signaling by the v-ErbB oncoprotein, we have investigated signaling pathways downstream of this transmembrane tyrosine kinase. In this report, we describe tissue-specific patterns of phosphotyrosyl proteins in three distinct cell types transformed by the v-erbB oncogene: fibroblasts, erythroblasts, and endothelial cells. In addition, we describe transformation-specific tyrosine phosphorylation events and signal complex formation in v-erbB-transformed fibroblasts. Two patterns of phosphotyrosyl proteins have been detected in v-erbB- transformed cells. The first is a fibroblast-specific pattern which includes unique phosphotyrosyl proteins of 170 kDa (c-ErbB1), 158 kDa, and 120 kDa (the catenin-like protein p120cas). The second is an erythroblast/endothelial cell-specific pattern which includes a prominent unidentified phosphotyrosyl protein of 120 kDa. Evaluation of the phosphotyrosyl proteins p120cas and SHC in chicken embryo fibroblasts infected with transforming and nontransforming v-erbB mutants reveals transformation-specific patterns of tyrosine phosphorylation. One corollary of these phosphorylation events in v- erbB-transformed fibroblasts is the formation of a complex involving SHC, growth factor receptor-bound protein 2, and a novel 75-kDa phosphotyrosyl protein. The results of these studies suggest that the v- ErbB oncoprotein can couple to multiple signal transduction pathways, that these pathways are tissue specific, and that v-erbB-mediated transformation involves specific tyrosine phosphorylation events.

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