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The GATOR2–mTORC2 axis mediates Sestrin2-induced AKT Ser/Thr kinase activation

Allison H. Kowalsky, Sim Namkoong, Eric Mettetal, Hwan‐Woo Park, Dubek Kazyken, Diane C. Fingar, Jun Hee Lee

2020Journal of Biological Chemistry56 citationsDOIOpen Access PDF

Abstract

kinase assay, indicating that mTORC2 may represent the major link between Sestrin2 and AKT. As reported previously, Sestrin2 interacted with mTORC2; however, we found here that this interaction occurs indirectly through GATOR2, a pentameric protein complex that directly interacts with Sestrin2. Deleting or silencing WDR24 (WD repeat domain 24), the GATOR2 component essential for the Sestrin2-GATOR2 interaction, or WDR59, the GATOR2 component essential for the GATOR2-mTORC2 interaction, completely ablated Sestrin2-induced AKT activation. We also noted that Sestrin2 also directly binds to the pleckstrin homology domain of AKT and induces AKT translocation to the plasma membrane. These results uncover a signaling mechanism whereby Sestrin2 activates AKT through GATOR2 and mTORC2.

Topics & Concepts

mTORC2Protein kinase BCell biologyChemistryPI3K/AKT/mTOR pathwayPhosphorylationmTORC1Signal transductionBiologyPI3K/AKT/mTOR signaling in cancerCRISPR and Genetic EngineeringCancer Mechanisms and Therapy