G蛋白βγ亚基对磷脂酰肌醇特异性磷脂酶C-β3的激活作用。
Activation of phosphatidylinositol lipid-specific phospholipase C-beta 3 by G-protein beta gamma subunits.
作者信息
Carozzi A, Camps M, Gierschik P, Parker P J
机构信息
Protein Phosphorylation Laboratory, Imperial Cancer Research Fund, Lincoln's Inn Fields, London, UK.
出版信息
FEBS Lett. 1993 Jan 11;315(3):340-2. doi: 10.1016/0014-5793(93)81190-b.
A novel member of the inositol lipid-specific phospholipase C family, PtdIns-PLC beta 3, is shown to be activated by beta gamma subunits of the heterotrimeric GTP-binding protein, transducin. The activation is a direct effect since it is observed with the purified proteins. Furthermore, the activation is blocked by the GDP-liganded alpha subunit of transducin, confirming that the effect is due to free beta gamma subunits. The implications with respect to receptor-PtdIns-PLC coupling are discussed.
肌醇脂质特异性磷脂酶C家族的一个新成员，磷脂酰肌醇磷脂酶Cβ3，被证明可被异源三聚体GTP结合蛋白转导素的βγ亚基激活。这种激活是直接作用，因为在纯化的蛋白质中观察到了这种现象。此外，转导素的GDP结合α亚基可阻断这种激活，证实这种作用是由游离的βγ亚基引起的。文中讨论了其与受体-磷脂酰肌醇磷脂酶C偶联的相关性。
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