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The structure and function of PKN, a protein kinase having a catalytic domain homologous to that of PKC

被引：131
作者：
Mukai, H [1 ]
机构：
[1] Kobe Univ, Biosignal Res Ctr, Nada Ku, Kobe, Hyogo 6578501, Japan
来源：
JOURNAL OF BIOCHEMISTRY | 2003年 / 133卷 / 01期
关键词：
fatty acid; PKN; PAK; PRK; Rho;
D O I：
10.1093/jb/mvg019
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：
PKN is a serine/threonine protein kinase that has a catalytic domain homologous to protein kinase C (PKC) family members and a unique regulatory region containing antiparallel coiled-coil (ACC) domains. PKN is the first identified serine/threonine protein kinase that can bind to and be activated by a small GTPase Rho, and it can also be activated by fatty acids such as arachidonic acid in vitro. PKN is widely distributed in various organisms such as mammal, frog, fly, and starfish. There are at least three different isoforms of PKN (PKNalpha/PAK-1/PRK-1, PKNbeta, and PRK2/PAK-2/ PKNgamma) in mammals, each of which shows different enzymological properties, tissue distribution, and varied functions.
引用
收藏
页码：17 / 27
页数：11
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