1992
AUTHORSCathy Pears , Nigel Goode , Peter J. Parker
ABSTRACTProtein kinase C (PKC) consists of a family of at least nine members which can be subdivided into two main groups on the basis of sequence homology. Modification is required for the enzyme to be functional as the primary translation product (~77kD) appears to express no kinase activity. PKC isolated from tissue sources is a phosphoprotein of a higher molecular weight (~80kD). Use of a kinase deficient mutant of PKC indicates that the primary translation product undergoes an initial phosphorylation by a separate kinase with subsequent autophosphorylation to generate the “mature” protein. The primary translation products expressed in E. coli bind phorbol esters with apparently normal affinity, consistent with this family forming a major class of phorbol ester receptors. Isolation of the individual isotypes of PKC from tissue sources or after expression of cDNA sequences in mammalian cells has revealed differences in substrate specificity and effector dependence of kinase activity. The fusion of regulatory and catalytic domains from different isotypes has revealed that the regions of the protein responsible for the limited substrate range of PKC-ε in vitro lie within the regulatory domain of the enzyme, suggesting a role for this region in limiting access to the active site. The substrate selectivity may be extended towards a physiologically relevant substrate. Activated versions of the various isotypes of PKC are being constructed by mutagenesis in order to study the functions of the individual isotypes following expression in mammalian cells. More... »
PAGES231-241
Adenine Nucleotides in Cellular Energy Transfer and Signal Transduction
ISBN
978-3-0348-7317-8
978-3-0348-7315-4
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