Historical Background
Protein kinase C was discovered in the late 1970s by Yasutomi Nishizuka and his team at Kobe University, Japan. They had originally purified a kinase that required only Mg2+ for activity, so they named it protein kinase M (PKM). It soon became apparent to the group that PKM was a proteolytic product of a larger enzyme whose kinase activity needed to be unmasked by cofactors. They named the parent enzyme protein kinase C because a Ca2+-dependent protease cleaved it to release the unregulated kinase moiety they had initially purified. The subsequent identification of diacylglycerol as the key cofactor provided an explanation for how lipid hydrolysis, discovered 25 years earlier to be triggered by stimuli such as acetylcholine, couples to intracellular signaling pathways. But the discovery that shot PKC into the limelight was its specific binding to, and activation by, tumor-promoting phorbol esters, a discovery that was facilitated by the synthesis of relatively...
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Newton, A.C. (2018). Protein Kinase C (Prkc). In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, Cham. https://doi.org/10.1007/978-3-319-67199-4_101822
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DOI: https://doi.org/10.1007/978-3-319-67199-4_101822
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