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J Biol Chem, Vol. 274, Issue 14, 9133-9136, April 2, 1999
with Regulatory Phosphorylation
Sites in the Activation Loop and in the C-terminal Hydrophobic
Domain
From the Friedrich Miescher-Institut, P. O. Box
2543, 4002 Basel, Switzerland
We have cloned human protein kinase B
(PKB)
and found that it contains two regulatory phosphorylation sites,
Thr305 and Ser472, which correspond to
Thr308 and Ser473 of PKB
. Thus it differs
significantly from the previously published rat PKB. We have also
isolated a similar clone from a mouse cDNA library. In human
tissues, PKB is widely expressed as two transcripts. A mutational
analysis of the two regulatory sites of human PKB showed that
phosphorylation of both sites, occurring in a phosphoinositide 3-kinase-dependent manner, is required for full activity.
Our results suggest that the two phosphorylation sites act in concert to produce full activation of PKB, similar to PKB. This contrasts with rat PKB, which is thought to be regulated by
3-phosphoinositide-dependent protein kinase 1 alone.
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