Tobin A B
Department of Cell Physiology and Pharmacology, University of Leicester, United Kingdom.
Pharmacol Ther. 1997 Aug;75(2):135-51. doi: 10.1016/s0163-7258(97)00053-3.
Early work on G-protein-coupled receptor (GPCR) phosphorylation focused on the adenylyl cyclase-linked beta-adrenoceptor, where phosphorylation at sites on the C-terminal tail and within the third intracellular loop results in receptor desensitisation. In recent years, intense research activity has revealed that a large number of GPCR subtypes exist as phosphoproteins, where the level of phosphorylation is dramatically increased subsequent to receptor stimulation. Among these receptor subtypes are those receptors coupled to phospholipase C (PLC). It appears, therefore, that regulation via receptor phosphorylation is a mechanism employed by all but a few GPCRs, including those coupled to PLC. Because the majority of GPCRs are coupled to the phosphoinositide signalling pathway, receptor phosphorylation of PLC-coupled receptors is a regulatory process with profound physiological significance for a huge array of biological responses. This review discusses the properties of homologous and heterologous phosphorylation of PLC-coupled receptors, together with the receptor kinases involved and the functional significance of receptor phosphorylation.
早期关于G蛋白偶联受体（GPCR）磷酸化的研究集中在与腺苷酸环化酶偶联的β-肾上腺素能受体上，其C末端尾巴和第三个细胞内环上位点的磷酸化会导致受体脱敏。近年来，大量研究活动表明，许多GPCR亚型以磷酸化蛋白形式存在，受体受到刺激后磷酸化水平会显著增加。这些受体亚型中包括与磷脂酶C（PLC）偶联的受体。因此，似乎除了少数GPCR（包括与PLC偶联的那些）外，通过受体磷酸化进行调节是所有GPCR都采用的一种机制。由于大多数GPCR与磷酸肌醇信号通路偶联，PLC偶联受体的受体磷酸化是一个对大量生物反应具有深远生理意义的调节过程。本文综述了PLC偶联受体的同源和异源磷酸化特性，以及涉及的受体激酶和受体磷酸化的功能意义。
