IndraLab

Statements

OTUB1 inhibits AKT. 6 / 6
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"In addition, Otub1 deletion in cells enhanced AKT activity, leading to a larger cell size, higher ATP levels and reduced AMPK phosphorylation."
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"IL-15 mediates membrane recruitment of Otub1, which inhibits ubiquitin-dependent activation of AKT, a pivotal kinase for T cell activation and metabolism."
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"Furthermore, Otub1 deficiency in NK cells also profoundly enhanced IL-15-stimulated activation of AKT, but not activation of STAT5 (Fig. 4c)."
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"Besides, when we blocked PI3K/AKT and/or MEK/ERK signaling by its specific inhibitor MK2206 and PD98059, the promotive effect of OTUB1-induced malignant behavior of HCC cells was also significantly reversed (Fig. 6d–q), demonstrating that OTUB1 performed the tumor-enhanced effects by effectively activating the AKT and ERK signaling pathway."
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"The PI3K and AKT pathway integrates the TCR and CD28 and IL-15R signals and is negatively regulated by the DUB Otub1."
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"We found that IL-15 stimulated membrane translocation of AKT, which was greatly enhanced by Otub1 knockdown (Fig. 5a)."
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