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.