Src家族蛋白酪氨酸激酶对PLC-γ1和PLC-γ2的体外酪氨酸磷酸化作用。
In vitro tyrosine phosphorylation of PLC-gamma 1 and PLC-gamma 2 by src-family protein tyrosine kinases.
作者信息
Liao F, Shin H S, Rhee S G
机构信息
Department of Molecular Biology and Genetics, Johns Hopkins University, School of Medicine, Baltimore, MD 21205.
出版信息
Biochem Biophys Res Commun. 1993 Mar 31;191(3):1028-33. doi: 10.1006/bbrc.1993.1320.
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.
我们在体外研究了src家族蛋白酪氨酸激酶（PTK）P56lck、p53/56lyn、p59hck、p59fyn和p60src对纯化的磷脂酶C-γ1（PLC-γ1）和磷脂酶C-γ2（PLC-γ2）的磷酸化作用。所有这五种PTK均能使PLC-γ1和PLC-γ2发生磷酸化，这表明在细胞表面受体激活后，这两种PLC-γ同工酶在细胞内均可被任何一种src家族PTK磷酸化。体外磷酸化速率的比较显示，PLC-γ1与PLC-γ2之间，以及这五种PTK之间均无明显的特异性。
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