The isoform-specific regulation of apoptosis by protein kinase C.
The process of apoptosis is regulated at several levels through phosphorylation by many different protein kinases. The protein kinase C (PKC) family, which comprises at least 10 isoforms with distinct means of regulation and tissue distribution patterns, have been shown to exert both inhibitory and stimulatory influences on apoptosis. This review details recent progress made in determining the roles played by individual PKC isoforms in the control of apoptosis, with reference to their target substrates and actions in different cell types. Although notable exceptions exist, the weight of evidence indicates that the alpha, beta, epsilon and atypical isoforms are anti-apoptotic in their action, whereas the delta and theta isoforms are usually involved in the promotion of apoptosis.
Gutcher
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I
School of Medicine, University of Manchester, G186 Stopford Building, Oxford Road, Manchester M13 9PT, United Kingdom.
Webb
P R
PR
Anderson
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NG
D000818:Animals; D017209:Apoptosis / Q000502:physiology*; D020169:Caspases / Q000502:physiology; D002470:Cell Survival / Q000502:physiology; D004789:Enzyme Activation; D006801:Humans; D007527:Isoenzymes / Q000737:chemistry / Q000502:physiology; D008954:Models, Biological; D010766:Phosphorylation; D011493:Protein Kinase C / Q000737:chemistry / Q000502:physiology*; D019014:fas Receptor / Q000502:physiology
D007527:Isoenzymes; D019014:fas Receptor; D011493:Protein Kinase C; D020169:Caspases