PT  - JOURNAL ARTICLE
AU  - Le Good, J. Ann
AU  - Ziegler, Wolfgang H.
AU  - Parekh, Davey B.
AU  - Alessi, Dario R.
AU  - Cohen, Philip
AU  - Parker, Peter J.
TI  - Protein Kinase C Isotypes Controlled by Phosphoinositide 3-Kinase Through the Protein Kinase PDK1
AID  - 10.1126/science.281.5385.2042
DP  - 1998 Sep 25
TA  - Science
PG  - 2042--2045
VI  - 281
IP  - 5385
4099  - http://science.sciencemag.org/content/281/5385/2042.short
4100  - http://science.sciencemag.org/content/281/5385/2042.full
SO  - Science1998 Sep 25; 281
AB  - Phosphorylation sites in members of the protein kinase A (PKA), PKG, and PKC kinase subfamily are conserved. Thus, the PKB kinase PDK1 may be responsible for the phosphorylation of PKC isotypes. PDK1 phosphorylated the activation loop sites of PKCζ and PKCδ in vitro and in a phosphoinositide 3-kinase (PI 3-kinase)–dependent manner in vivo in human embryonic kidney (293) cells. All members of the PKC family tested formed complexes with PDK1. PDK1-dependent phosphorylation of PKCδ in vitro was stimulated by combined PKC and PDK1 activators. The activation loop phosphorylation of PKCδ in response to serum stimulation of cells was PI 3-kinase–dependent and was enhanced by PDK1 coexpression.