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| biopax3:comment |
Signaling by AKT is one of the key outcomes of activation of receptor tyrosine kinases (RTKs). Following ligand binding and autophosphorylation, RTKs recruit the 85 kDa regulatory subunit of PI3K (PIK3), PI3KR1 (also known as PI3K p85), either directly or indirectly, through adaptor proteins. The RTK-associated PI3KR1 recruits the 110 kDa catalytic subunit of PI3K, PI3KCA (also known as PI3K p110), resulting in the assembly of an active PI3K complex. Active PI3K phosphorylates PIP2, converting it to PIP3. PIP3 formation is negatively regulated by the PTEN tumor suppressor protein, a phosphatase that dephosphorylates PIP3 and coverts it to PIP2. PIP3 recruits AKT and PDK1 to the plasma membrane, enabling the PDK1 to phosphorylate AKT on a conserved threonine residue. AKT is also phosphorylated on a conserved serine residue by the TORC2 complex (also activated as a consequence of RTK signaling). Both the threonine and the serine residue need to be phosphorylated in order for the AKT to become fully active. The active AKT dissociates from the PIP3, and phosphorylates a number of cytosolic and nuclear proteins that play important roles in cell survival and metabolism. For a recent review of AKT signaling, please refer to Manning and Cantley, 2007.
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PIP3 activates AKT signaling
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| biopax3:pathwayComponent |
http://www.reactome.org/biopax/48887BiochemicalReaction1616,
http://www.reactome.org/biopax/48887BiochemicalReaction1617,
http://www.reactome.org/biopax/48887BiochemicalReaction1626,
http://www.reactome.org/biopax/48887BiochemicalReaction930,
http://www.reactome.org/biopax/48887Pathway430,
http://www.reactome.org/biopax/48887Pathway431,
http://www.reactome.org/biopax/48887Pathway432
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