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kin(p(HGNC:PDPK1)) => kin(p(HGNC:AKT2))
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Approximately 61,000 statements.
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Copyright (c) 2011-2012, Selventa. All rights reserved.
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BEL Framework Large Corpus Document
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1.4
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identified four sites (Ser-124, Thr-308, Thr-450, and Ser-473) on Akt1 that are phosphorylated in vivo. Thr-308 and Ser-473 are inducibly phosphorylated after treatment of cells with extracellular stimuli, whereas Ser-124 and Thr-450 appear to be basally phosphorylated The third mechanism by which 3'-phosphorylated phosphoinositides regulate Akt activity is by controlling the accessibility of Akt as a substrate for PDKs. In in vitro reconstitution assays, the binding of PI3,4,5P to the Akt PH domain is required for PDK-1 to phosphorylate Akt In addition, PDK-1 complexed with either a fragment of PRK2, PRK2, or a PRK2-related peptide may be regulated by increased phospholipid concentrations
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Selventa
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2014-07-03T14:29:49.379+02:00
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