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The PKC family of serine/threonine kinases, including PRKCE (PKC epsilon), is activated intracellularly by signal transduction pathways. In humans, at least 12 different PKC polypeptides have been identified. These isoforms differ in primary structure, tissue distribution, subcellular localization, mode of action in vitro, response to extracellular signals, and substrate specificity. PKC alpha, beta I, beta II, and gamma form the conventional family; their activities are Ca2+- and phospholipid-dependent. Protein kinase C (PKC) can be activated by calcium and second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role in cells.
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