Le Good J A, Ziegler W H, Parekh D B, Alessi D R, Cohen P, Parker P J
Protein Phosphorylation Laboratory, Imperial Cancer Research Fund, 44 Lincoln's Inn Fields, London WC2A 3PX, UK.
Science. 1998 Sep 25;281(5385):2042-5. doi: 10.1126/science.281.5385.2042.
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 PKCzeta and PKCdelta 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 PKCdelta in vitro was stimulated by combined PKC and PDK1 activators. The activation loop phosphorylation of PKCdelta in response to serum stimulation of cells was PI 3-kinase-dependent and was enhanced by PDK1 coexpression.
蛋白激酶A（PKA）、蛋白激酶G（PKG）和蛋白激酶C（PKC）激酶亚家族成员中的磷酸化位点是保守的。因此，蛋白激酶B激酶PDK1可能负责PKC同种型的磷酸化。PDK1在体外以及在人胚肾（293）细胞体内以磷酸肌醇3激酶（PI 3激酶）依赖性方式磷酸化PKCζ和PKCδ的激活环位点。所测试的PKC家族的所有成员均与PDK1形成复合物。PKC和PDK1激活剂联合使用可刺激体外PDK1依赖性的PKCδ磷酸化。细胞经血清刺激后，PKCδ的激活环磷酸化是PI 3激酶依赖性的，并且通过共表达PDK1而增强。
