Abstract
The phosphorylation of purified phospholipase C-gamma 1 (PLC-gamma 1) and PLC-gamma 2 by src-family-protein tyrosine kinases (PTKs) P56lck, p53/56lyn, p59hck, p59fyn, and p60src was studied in vitro. All five PTKs phosphorylated PLC-gamma 1 and PLC-gamma 2, suggesting that both PLC-gamma isozymes can be phosphorylated in cells by any of the src-family PTKs in response to the activation of cell surface receptors. Comparison of the in vitro phosphorylation rates revealed no distinct specificity between PLC-gamma 1 and PLC-gamma 2, or between the five PTKs.
MeSH terms
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Humans
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In Vitro Techniques
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Isoenzymes / metabolism
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Phosphotyrosine
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Protein-Tyrosine Kinases / metabolism*
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Proto-Oncogene Proteins / metabolism
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Proto-Oncogene Proteins c-fyn
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Proto-Oncogene Proteins c-hck
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Proto-Oncogene Proteins pp60(c-src) / metabolism
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Tumor Cells, Cultured
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Type C Phospholipases / metabolism*
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Tyrosine / analogs & derivatives*
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Tyrosine / metabolism
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src-Family Kinases*
Substances
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Isoenzymes
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Proto-Oncogene Proteins
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Phosphotyrosine
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Tyrosine
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Protein-Tyrosine Kinases
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FYN protein, human
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HCK protein, human
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Proto-Oncogene Proteins c-fyn
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Proto-Oncogene Proteins c-hck
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Proto-Oncogene Proteins pp60(c-src)
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lyn protein-tyrosine kinase
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src-Family Kinases
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Type C Phospholipases