G蛋白βγ亚基拮抗蛋白激酶C依赖性磷酸化并抑制磷脂酶C-β1。
G-protein betagamma subunits antagonize protein kinase C-dependent phosphorylation and inhibition of phospholipase C-beta1.
作者信息
Litosch I
机构信息
Department of Molecular and Cellular Pharmacology, University of Miami School of Medicine, Miami, FL 33101, USA.
出版信息
Biochem J. 1997 Sep 15;326 ( Pt 3)(Pt 3):701-7. doi: 10.1042/bj3260701.
Abstract
Protein kinase C (PKC) isoforms phosphorylated phospholipase C-beta1 (PLC-beta1) in vitro as follows: PKCalpha >> PKCepsilon; not PKCzeta. PLC-beta3 was not phosphorylated by PKCalpha. G-protein betagamma subunits inhibited the PKCalpha phosphorylation of PLC-beta1 in a concentration-dependent manner. Half-maximal inhibition occurred with 500 nM betagamma. G-protein betagamma subunits also antagonized the PKCalpha-mediated inhibition of PLC-beta1 enzymic activity. PKCalpha, in turn, inhibited the stimulation of PLC-beta1 activity by betagamma. There was little effect of PKCalpha on the stimulation of PLC-beta1 by alphaq/11-guanosine 5'[gamma-thio]triphosphate (GTP[S]). These findings demonstrate that G protein betagamma subunits antagonize PKCalpha regulation of PLC-beta1. Thus betagamma subunits might have a role in modulating the negative feedback regulation of this signalling system by PKC.
摘要
蛋白激酶C（PKC）同工型在体外对磷脂酶C-β1（PLC-β1）进行磷酸化的情况如下：PKCα >> PKCε；PKCζ无此作用。PKCα不使PLC-β3磷酸化。G蛋白βγ亚基以浓度依赖性方式抑制PKCα对PLC-β1的磷酸化。500 nM的βγ可产生半数最大抑制作用。G蛋白βγ亚基还拮抗PKCα介导的对PLC-β1酶活性的抑制。反过来，PKCα抑制βγ对PLC-β1活性的刺激。PKCα对αq/11-鸟苷5'-[γ-硫代]三磷酸（GTP[S]）刺激PLC-β1的作用影响很小。这些发现表明G蛋白βγ亚基拮抗PKCα对PLC-β1的调节。因此，βγ亚基可能在调节PKC对该信号系统的负反馈调节中发挥作用。
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