EXPRESSION, PURIFICATION AND CHARACTERIZATION OF THE UBIQUITOUS PROTEIN-KINASE-C-RELATED KINASE-1

被引：34

作者：

PALMER, RH ^{[1
]}

PARKER, PJ ^{[1
]}

机构：

[1] IMPERIAL CANC RES FUND,LONDON WC2A 3PX,ENGLAND

来源：

BIOCHEMICAL JOURNAL | 1995年 / 309卷

关键词：

D O I：

10.1042/bj3090315

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.-

引用

页码：315 / 320

页数：6

共 15 条

[1] SUBSTRATE-SPECIFIC STIMULATION OF PROTEIN-KINASE-C BY POLYVALENT ANIONS [J].