J. Biochem, 2003, Vol. 133, No. 1 17-27
© 2003 Japanese Biochemical Society
JB MINIREVIEWS |
The Structure and Function of PKN, a Protein Kinase Having a Catalytic Domain Homologous to That of PKC
Biosignal Research Center, Kobe University, 1-1 Rokkodai-cho, Nada-ku, Kobe 657-8501
ABSTRACT
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 (PKN
/PAK-1/PRK-1, PKNß, and PRK2/PAK-2/PKN
) in mammals, each of which shows different enzymological properties, tissue distribution, and varied functions.
FOOTNOTES
+ To whom correspondence should be addressed. Tel: +81-78-803-6467, Fax: +81-78-803-5782, E-mail: mukinase{at}kobe-u.ac.jp
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