Abstract
In this paper we demonstrate the presence of two novel in vivo autophosphorylation sites in the c-Kit/stem cell factor receptor (c-Kit/SCFR): Tyr-703 in the kinase insert and Tyr-936 in the C-terminal tail. We furthermore demonstrate that the adapter protein Grb2 is a specific binding partner for both phosphorylated Tyr-703 and phosphorylated Tyr-936, whereas the adapter protein Grb7 binds selectively to phosphorylated Tyr-936. It is shown that the association occurs through the Src homology 2 (SH2) domains of Grb2 and Grb7. Binding of Grb2 to Tyr-703 in the c-Kit/SCFR provides a link to the Ras/mitogen-activated protein kinase pathway.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adaptor Proteins, Signal Transducing*
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Cells, Cultured
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Endothelium, Vascular / cytology
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GRB2 Adaptor Protein
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GRB7 Adaptor Protein
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Humans
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Phosphorylation
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Protein Binding
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Proteins / metabolism*
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Proto-Oncogene Proteins c-kit / genetics
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Proto-Oncogene Proteins c-kit / metabolism*
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Receptor Protein-Tyrosine Kinases / genetics
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Receptor Protein-Tyrosine Kinases / metabolism
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Recombinant Fusion Proteins / metabolism
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Stem Cell Factor
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Tyrosine*
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src Homology Domains
Substances
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Adaptor Proteins, Signal Transducing
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GRB2 Adaptor Protein
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GRB2 protein, human
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GRB7 protein, human
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Proteins
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Recombinant Fusion Proteins
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Stem Cell Factor
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GRB7 Adaptor Protein
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Tyrosine
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Proto-Oncogene Proteins c-kit
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Receptor Protein-Tyrosine Kinases