descriptionPublicationkeyboard_double_arrow_right Article 01 Mar 1993 English Publisher:Elsevier BVJournal:Biochemical and Biophysical Research Communications, volume 191, pages 1,028-1,033 (issn: 0006-291X,

Authors: F, Liao; H S, Shin; S G, Rhee;

doi: 10.1006/bbrc.1993.1320

pmid: 7682059

In Vitro Tyrosine Phosphorylation of PLC-γ1 and PLC-γ2 by SRC-Family Protein Tyrosine Kinases

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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.

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Johns Hopkins University
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Johns Hopkins Medicine
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Johns Hopkins University School of Medicine
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Keywords

Proto-Oncogene Proteins pp60(c-src), In Vitro Techniques, Protein-Tyrosine Kinases, Proto-Oncogene Proteins c-fyn, Isoenzymes, src-Family Kinases, Proto-Oncogene Proteins, Type C Phospholipases, Proto-Oncogene Proteins c-hck, Tumor Cells, Cultured, Humans, Tyrosine, Phosphotyrosine

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