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Shc proteins are phosphorylated and regulated by the v-Src and v-Fps protein-tyrosine kinases.

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Shc proteins are phosphorylated and regulated by the v-Src and v-Fps protein-tyrosine kinases.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Pelicci, G. Mcglade, J. Pelicci, P. G. Pawson, T. Cheng, A.
Description	Author Affiliation: McGlade J ( Division of Molecular and Developmental Biology, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, ON, Canada.);
Abstract	The mammalian shc gene encodes two overlapping proteins of 46 and 52 kDa, each with a C-terminal Src homology 2 (SH2) domain and an N-terminal glycine/proline-rich sequence, that induce malignant transformation when overexpressed in mouse fibroblasts. p46shc, p52shc, and an additional 66-kDa shc gene product become highly tyrosine phosphorylated in Rat-2 cells transformed by the v-src or v-fps oncogene. Experiments using temperature-sensitive v-src and v-fps mutants indicate that Shc tyrosine phosphorylation is rapidly induced upon activation of the v-Src or v-Fps tyrosine kinases. These results suggest that Shc proteins may be directly phosphorylated by the v-Src and v-Fps oncoproteins in vivo. In cells transformed by v-src or v-fps, or in normal cells stimulated with epidermal growth factor, Shc proteins complex with a poorly phosphorylated 23-kDa polypeptide (p23). Activated tyrosine kinases therefore regulate the association of Shc proteins with p23 and may thereby control the stimulation of an Shc-mediated signal transduction pathway. The efficient phosphorylation of Shc proteins and the apparent induction of their p23-binding activity in v-src- and v-fps-transformed cells are consistent with the proposition that the SH2-containing Shc polypeptides are biologically relevant substrates of the oncogenic v-Src and v-Fps tyrosine kinases.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	19
Volume Number	89
Language	English
Publisher	National Academy of Sciences
Publisher Date	1992-11-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Genes, Src Oncogene Protein Pp60(v-src) Metabolism Oncogene Proteins V-fos Oncogenes Phosphoproteins Protein-Tyrosine Kinases Animals Cell Line, Transformed Electrophoresis, Polyacrylamide Gel Molecular Weight Genetics Phosphates Isolation & Purification Phosphorus Radioisotopes Phosphorylation Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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