Journal
JOURNAL OF BIOCHEMISTRY
Volume 132, Issue 6, Pages 831-839Publisher
OXFORD UNIV PRESS
DOI: 10.1093/oxfordjournals.jbchem.a003294
Keywords
diacylglycerol; phorbol ester; PKC delta; proteolysis; tyrosine phosphorylation
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Protein kinase C (PKC)delta was the first new/novel PKC isoform to be identified by the screening of mammalian cDNA libraries, based on the structural homology of its nucleotide sequences with those of classical/conventional PKC isoforms. PKCdelta is expressed ubiquitously among cells and tissues. It is activated by diacylglycerol produced by receptor-mediated hydrolysis of membrane inositol phospholipids as well as by tumor-promoting phorbol ester through the binding of these compounds to the C1 region in its regulatory domain. It is,also cleaved by caspase to generate a catalytically active fragment, and it is converted to an active form without proteolysis through the tyrosine phosphorylation reaction. Various lines of evidence indicate that PKCdelta activated in distinct ways plays critical roles in cellular functions such as the control of growth, differentiation, and apoptosis. This article briefly summarizes the regulatory mechanisms of PKCdelta activity and its functions in cell signaling.
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