Abstract
The discovery of protein kinase C (PKC) found nearly two decades ago opened a new research field of signal transduction. A lipid product, diacylglycerol (DG) that is produced from signal-induced hydrolysis of inositol phospholipid by phospholipase C (PLC), triggers the activation of this enzyme (Nishizuka, 1984). Since then, knowledge of the PKC family consisting of multiple isoforms and its related enzymes has expanded rapidly (Nishizuka, 1988). Today, it is clear that the activation of the PKC family is coupled to the dynamic metabolism of various membrane phospholipids. Lipid-induced targeting of each isoform to selective intracellular compartments represent an essential step for stable access to the substrate proteins, and thus for revealing isoform-specific biological functions.
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