The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
The Structure and Function of PKN, a Protein Kinase Having a Catalytic Domain Homologous to That of PKC
Hideyuki Mukai
著者情報
キーワード: fatty acid, PKN, PAK, PRK, Rho
ジャーナル フリー

2003 年 133 巻 1 号 p. 17-27

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抄録
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 (PKNα/PAK-1/PRK-l, PKNβ, and PRK2/PAK-2/ PKNγ) in mammals, each of which shows different enzymological properties, tissue distribution, and varied functions.
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© The Japanese Biochemical Society
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