PDPK1 phosphorylates AKT at T308 Authored: Nasi, S, Annibali, D, 2006-10-10 09:07:07 EC Number: 2.7.11 Edited: Matthews, L, 2012-08-03 Once AKT is localized at the plasma membrane, it is phosphorylated at two critical residues for its full activation. These residues are a threonine (T308 in AKT1) in the activation loop within the catalytic domain, and a serine (S473 in AKT1), in a hydrophobic motif (HM) within the carboxy terminal, non-catalytic region. PDPK1 (PDK1) is the activation loop kinase; this kinase can also directly phosphorylate p70S6K. The HM kinase, previously termed PDK2, has been identified as the mammalian TOR (Target Of Rapamycin; Sarbassov et al., 2005) but several other kinases are also able to phosphorylate AKT at S473. Phosphorylation of AKT at S473 by TORC2 complex is a prerequisite for PDPK1-mediated phosphorylation of AKT threonine T308 (Scheid et al. 2002, Sarabassov et al. 2005). Pubmed7637810 Pubmed9736715 Reactome Database ID Release 43198270 Reactome, http://www.reactome.org ReactomeREACT_12584 Reviewed: Greene, LA, 2007-11-08 15:39:37 Reviewed: Thorpe, Lauren, 2012-08-13 Reviewed: Yuzugullu, Haluk, 2012-08-13 Reviewed: Zhao, Jean J, 2012-08-13 PDK1:PIP3 p-S-AKT:PDPK1:PIP3 p-AKT