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. 1995 Jul 1;309 ( Pt 1)(Pt 1):315-20.
doi: 10.1042/bj3090315.

Expression, purification and characterization of the ubiquitous protein kinase C-related kinase 1

R H Palmer  1 , P J Parker
Affiliations

Expression, purification and characterization of the ubiquitous protein kinase C-related kinase 1

R H Palmer et al. Biochem J. .

Abstract

The recently described protein kinase C-related kinase (PRK) family is comprised of at least three members: PRK1, PRK2 and PRK3. Here the expression, purification and characterization of the ubiquitously expressed isoform, PRK1, is described. The enzyme was expressed in COS 7 cells and subsequently purified to apparent homogeneity by sequential column chromatography. The purified PRK1 protein migrates as a single 120 kDa polypeptide on SDS/PAGE. It displays a substrate specificity that in part resembles that of protein kinase C (PKC); however, unlike PKC, it is not activated by any combination of phorbol esters, diacylglycerol and Ca2+. Nevertheless, it can be activated by limited proteolysis, indicating a negative regulatory role for the N-terminal domain(s). PRK1 is also activated by phospholipids. The physiological relevance of this activation is discussed.

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