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Protein Kinase C (PKC) refers to a family of serine/threonine kinases that play crucial roles in cellular signaling. The calcium-dependent isoforms (cPKCs), including α, βI, βII, and γ, require both calcium ions and diacylglycerol (DAG) for activation. Activation involves calcium binding to the C2 domain, promoting membrane association, followed by DAG binding to the C1 domains, leading to kinase activation and substrate phosphorylation. cPKCs regulate diverse cellular processes including cell cycle progression, proliferation, differentiation, and apoptosis. They are implicated in diseases like cancer due to their role in proliferation/apoptosis balance and are also involved in neuronal synaptic plasticity.
PKC activators (e.g., phorbol esters) bind to the C1 domain, mimicking DAG and activating the kinase. PKC inhibitors block kinase activity.
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