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The Akt pathway can be activated through inactivation and downregulation of its negative regulator, PTEN [17].
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Additionally, PI3K can be activated through genetic or epigenetic inactivation of PTEN.
PI3K can be activated through many mechanisms other than mutations, and loss of negative feedback loops such as inactivation of PTEN (phosphatase and tensin homolog deleted on chromosome 10) can also activate this complex pathway [ 32].
The regulation of mTOR is complex, but in summary, AKT, a serine threonine kinase, can be activated through a number of mechanisms, including the binding of a variety of growth factors to tyrosine kinase receptors, resulting in the phosphorylation of PI3K and PDK1 and subsequent inactivation of TSC1/TSC2 function, through phosphorylation of TSC2 at threonine 1462 by AKT.
Its protein product cannot be activated through Tyr phosphorylation.
Nonetheless, presumably the inactivation of Gwl requires active/reactivated PP2A-B55, because Gwl is activated through direct phosphorylation by CDK1 (as previously reported by the authors).
Wnt signaling is activated through cytoplasmic β-catenin.
The substrate is activated through protonation by a conserved tyrosine.
Monocytes/macrophages were activated through the physiological CD23 pathway [ 22].
NFκB is activated through the upstream kinase TAK1.
The extrinsic pathway is activated through the death receptors (DRs).
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