IndraLab

Statements


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"The Otub1-AKT binding was also readily detected under transfection conditions ( xref )."

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"Interestingly, AKT was physically associated with Otub1 in 15R-KIT cells, which was strongly enhanced upon IL-15 stimulation ( xref )."

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"In primary OT-I CD8 T cells, the AKT-Otub1 interaction was barely detectable at steady state but was strongly induced by IL-15 ( xref )."

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"IL-15-stimulated AKT activation is negatively regulated by Otub1, which physically interacts with AKT and prevents its K63 ubiquitination and membrane translocation. xref Interestingly, in IL-15-exposed cells, Otub1 is relocated to the membrane compartment, a mechanism that enables Otub1 to inhibit AKT ubiquitination and activation induced by both IL-15 and TCR signals (Fig. xref )."

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"Mechanistically, IL-15 strongly induces the interaction between Otub1 and AKT, inhibiting the K63-linked ubiquitination of AKT."