The structure and function of PKN, a protein kinase having a catalytic domain homologous to that of PKC.
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.
Mukai
Hideyuki
H
Biosignal Research Center, Kobe University, 1-1 Rokkodai-cho, Nada-ku, Kobe 657-8501. mukinase@kobe-u.ac.jp
D000818:Animals; D017209:Apoptosis; D020134:Catalytic Domain; D002448:Cell Adhesion; D002874:Chromosome Mapping; D003599:Cytoskeleton / Q000378:metabolism; D006801:Humans; D008540:Meiosis; D051379:Mice; D011493:Protein Kinase C / Q000737:chemistry* / Q000502:physiology*; D012333:RNA, Messenger / Q000235:genetics; D051381:Rats; D017386:Sequence Homology, Amino Acid; D022161:Transport Vesicles / Q000201:enzymology
D012333:RNA, Messenger; C061570:protein kinase N; D011493:Protein Kinase C