The conventional Protein Kinase C (cPKC) isoforms have two membrane-targetting domains, a C1 domain which binds to the membrane lipid diacylglycerol (DAG) and a C2 domain which binds membrane phospholipids such as phosphatidylserine, in a calcium-dependent manner. Association of both domains with the plasma membrane produces a conformational change that releases an autoinhibitory pseudosubstrate segment from the substrate-binding cavity, allowing substrate binding and downstream signaling.
Oancea, E, Meyer, T
Protein Kinase C (PKC) is positively regulated by events that increase the plasma membrane concentration of diacylglycerol (DAG). Activation of PKC requires the coordinated binding of two membrane-targeting domains. The C1 domain binds diacylglycerol, the C2 domain binds phosphatidylserine. Each can bind the membrane independently, but with insufficient affinity for membrane recruitment and activation.
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