Artigo Acesso aberto Revisado por pares

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

1993; Elsevier BV; Volume: 191; Issue: 3 Linguagem: Inglês

10.1006/bbrc.1993.1320

ISSN

1090-2104

Autores

Fang Liao, H S Shin, Sue Goo Rhee,

Tópico(s)

Chronic Myeloid Leukemia Treatments

Resumo

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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