Reversible exposure of the pseudosubstrate domain of protein kinase C by phosphatidylserine and diacylglycerol.

摘要: The lipid activators of protein kinase C, phosphatidylserine and diacylglycerol, induce a reversible conformational change that exposes the auto-inhibitory pseudosubstrate domain enzyme. beta-II C is cleaved after first residue, arginine 19, by endoproteinase Arg-C only when bound to activating phosphatidylserine. Exposure this residue markedly enhanced diacylglycerol. In contrast, not in absence lipids, non-activating acidic has autophosphorylated on amino terminus, or dilution lipids. This work reveals specificity interaction with since phospholipid causes specific detected regulatory enzyme, demonstrates allosteric regulators expose intramolecular kinase.