Corbalán-García Senena, Gómez-Fernández Juan C
Departamento de Bioquímica y Biología Molecular-A, Regional Campus of International Excellence "Campus Mare Nostrum", Universidad de Murcia, Apartado de Correos 4021, 30080, Murcia, Spain.
Biophys Rev. 2014 Mar;6(1):3-14. doi: 10.1007/s12551-013-0125-z. Epub 2013 Nov 27.
Classical protein kinase C (PKC) enzymes are known to be important factors in cell physiology both in terms of health and disease. They are activated by triggering signals that induce their translocation to membranes. The consensus view is that several secondary messengers are involved in this activation, such as cytosolic Ca and diacylglycerol. Cytosolic Ca bridges the C2 domain to anionic phospholipids as phosphatidylserine in the membrane, and diacylglycerol binds to the C1 domain. Both diacylglycerol and the increase in Ca concentration are assumed to arise from the extracellular signal that triggers the hydrolysis of phosphatidylinositol-4,5-bisphosphate. However, results obtained during the last decade indicate that this phosphoinositide itself is also responsible for modulating classical PKC activity and its localization in the plasma membrane.
经典蛋白激酶C（PKC）酶无论是在健康还是疾病方面，都是细胞生理学中的重要因素。它们通过触发诱导其转位至细胞膜的信号而被激活。普遍的观点是，几种第二信使参与了这种激活过程，如胞质Ca和二酰基甘油。胞质Ca将C2结构域与膜中的阴离子磷脂（如磷脂酰丝氨酸）相连，而二酰基甘油则与C1结构域结合。二酰基甘油和Ca浓度的增加都被认为源于触发磷脂酰肌醇-4,5-二磷酸水解的细胞外信号。然而，过去十年间获得的结果表明，这种磷酸肌醇本身也负责调节经典PKC的活性及其在质膜中的定位。
