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

H Mukai - The Journal of Biochemistry, 2003 - jstage.jst.go.jp
H Mukai
The Journal of Biochemistry, 2003jstage.jst.go.jp
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
thatcan 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 dis tributed in various organisms such
as mammal, frog, fly, and starfish. There are at least three different isoforms of PKN …
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 thatcan 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 dis tributed in various organisms such as mammal, frog, fly, and starfish. There are at least three different isoforms of PKN (PKNa/PAK-1/PRK-l, PKNp, and PRK2/PAK-2/PKNy) in mammals, each of which shows different enzymological properties, tissue distribution, and varied functions.
jstage.jst.go.jp