Mechanism of phosphorylation of protein kinase B/Akt by a constitutively active 3-phosphoinositide-dependent protein kinase-1
MJ Wick, LQ Dong, RA Riojas, FJ Ramos… - Journal of Biological …, 2000 - ASBMB
Phosphorylation of Thr 308 in the activation loop and Ser 473 at the carboxyl terminus is
essential for protein kinase B (PKB/Akt) activation. However, the biochemical mechanism of
the phosphorylation remains to be characterized. Here we show that expression of a
constitutively active mutant of mouse 3-phosphoinositide-dependent protein kinase-1 (PDK1
A280V) in Chinese hamster ovary cells overexpressing the insulin receptor was sufficient to
induce PKB phosphorylation at Thr 308 to approximately the same extent as insulin …
essential for protein kinase B (PKB/Akt) activation. However, the biochemical mechanism of
the phosphorylation remains to be characterized. Here we show that expression of a
constitutively active mutant of mouse 3-phosphoinositide-dependent protein kinase-1 (PDK1
A280V) in Chinese hamster ovary cells overexpressing the insulin receptor was sufficient to
induce PKB phosphorylation at Thr 308 to approximately the same extent as insulin …
