Quest A F
Institute of Biochemistry, University of Lausanne, Epalinges, Switzerland.
Enzyme Protein. 1996;49(5-6):231-61. doi: 10.1159/000468635.
Protein kinase C (PKC) is a family of serine/threonine kinases implicated in intracellular signalling events triggered in response to a large variety of agonists. Currently, 11 mammalian PKC isoforms have been identified which are divided into three groups, the calcium-dependent, the non-calcium-dependent and the atypical isoforms. Common to all members is the presence of an aminoterminal regulatory domain, which renders the kinase inactive by interacting with the carboxyterminal catalytic domain. Thus, intracellular PKC activation requires the release of this autoinhibitory restraint, which, as this review summarizes, may involve both interactions with lipids and proteins. Furthermore, post-translational PKC phosphorylation events, required to convert PKC to an activation competent state, are discussed.
蛋白激酶C（PKC）是一类丝氨酸/苏氨酸激酶家族，参与由多种激动剂引发的细胞内信号转导事件。目前，已鉴定出11种哺乳动物PKC亚型，它们被分为三组：钙依赖性、非钙依赖性和非典型亚型。所有成员的共同特征是存在一个氨基末端调节结构域，该结构域通过与羧基末端催化结构域相互作用使激酶失活。因此，细胞内PKC的激活需要解除这种自抑制限制，如本综述所述，这可能涉及与脂质和蛋白质的相互作用。此外，还讨论了将PKC转化为激活状态所需的翻译后磷酸化事件。
