Getting to know protein kinase D.
The protein kinase D (PKD) enzymes represent a new family of second messenger stimulated kinases, with diacylglycerol as a prime, but not the sole, mediator of activation. Their molecular architecture features a catalytic domain, unrelated to that of all PKC family members, and a large inhibitory, regulatory domain, comprised of two Zinc fingers, and a pleckstrin homology domain. These different sub-domains play distinctive roles in the activation, translocation and biological functions of the kinase. The enzymes have been implicated in signalling mechanisms controlling cell proliferation and programmed cell death and in metastasis, immune responses, and Golgi restructuring and function. A variety of proteins specifically interact with the different sub-domains of the enzymes and direct their wide range of cellular functions.
Lint
Johan Van
JV
Division of Biochemistry, Faculty of Medicine, Campus Gasthuisberg, Katholieke Universiteit Leuven, Leuven, B-3000, Leuven, Belgium. johan.vanlint@med.kuleuven.ac.be
Rykx
An
A
Vantus
Tibor
T
Vandenheede
Jackie R
JR
D000595:Amino Acid Sequence; D000818:Animals; D001692:Biological Transport; D017124:Conserved Sequence; D004789:Enzyme Activation; D006801:Humans; D010766:Phosphorylation; D017354:Point Mutation; D011485:Protein Binding; D011493:Protein Kinase C / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D017384:Sequence Deletion; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction; D013329:Structure-Activity Relationship
C089212:protein kinase D; D011493:Protein Kinase C