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http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://purl.org/dc/elements/1.1/rights Copyright (c) 2011-2012, Selventa. All rights reserved. http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://purl.org/dc/elements/1.1/title BEL Framework Large Corpus Document http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://purl.org/pav/authoredBy http://www.tkuhn.ch/bel2nanopub/RAteI6bSZNeBCCfIBWqjrfsxtRnhM8IoNTrbnXGo7o1Ns#_8 http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://purl.org/pav/version 20131211 http://www.tkuhn.ch/bel2nanopub/RAteI6bSZNeBCCfIBWqjrfsxtRnhM8IoNTrbnXGo7o1Ns#_7 http://www.w3.org/ns/prov#value Akt/PKB is a member of the AGC kinase family, which also includes S6K, RSK, SGK, and PKC (Peterson and Schreiber, 1999; Woodgett, 2005). Most members of this family, including Akt, are phosphorylated at two key residues located at the catalytic site (activation loop or Tloop) and the C-terminal hydrophobic motif (HM) site. Phosphorylation of the HM site promotes docking of the PIF pocket of PDK1 to the HM site and concomitantly leads to the phosphorylation of the T-loop site upon growth factor stimulation and PI3K activation (Biondi, 2004). PDK1 phosphorylates Akt/PKB at Thr308 of its T loop, which is essential for Akt catalytic activity (Alessi et al., 1997; Stephens et al., 1998). As with many members of the AGC kinase family, HM phosphorylation of Akt at Ser473 and T-loop Thr308 phosphorylation has been proposed to be interdependent on each other (Scheid et al., 2002; Toker and Newton, 2000), although there is some opposing evidence (Alessi et al., 1996; Collins et al., 2003; Woodgett, 2005). For example, cells expressing a PDK1 mutant with a defective PIF pocket can still phosphorylate Akt (Biondi et al., 2001; Collins et al., 2003). Moreover, the HM of Akt also displays lower affinity for the PIF pocket of PDK1 in comparison to other PDK1 targets (Frodin et al., 2002). 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