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• W2034231497 abstract "The homeostasis of protein metabolism is maintained and regulated by the rates of protein biosynthesis and degradation in living systems. Alterations of protein degradation may regulate protein biosynthesis through a feedback mechanism. Whether a change in protein biosynthesis modulates protein degradation has not been reported. In this study, we found that inhibition of protein biosynthesis induced phosphorylation/activation of AKT and led to phosphorylation of AKT target substrates, including FoxO1, GSK3α/β, p70S6K, AS160, and the E3 ubiquitin ligase MDM2. Phosphorylation of ribosomal protein S6 was also modulated by inhibition of protein biosynthesis. The AKT phosphorylation/activation was mediated mainly through the PI3K pathway because it was blocked by the PI3K inhibitor LY294002. The activated AKT phosphorylated MDM2 at Ser166 and promoted degradation of the tumor suppressor p53. These findings suggest that inhibition of protein biosynthesis can alter degradation of some proteins through activation of AKT. This study reveals a novel regulation of protein degradation and calls for caution in blocking protein biosynthesis to study the half-life of proteins.Background: Whether a change in protein biosynthesis modulates protein degradation is unknown.Results: Inhibition of protein biosynthesis induces activation of AKT (protein kinase B), leading to activation of E3 ubiquitin ligase and thus degradation of its substrate proteins.Conclusion: Protein degradation is regulated by protein biosynthesis.Significance: This study reveals a novel regulation of protein degradation. The homeostasis of protein metabolism is maintained and regulated by the rates of protein biosynthesis and degradation in living systems. Alterations of protein degradation may regulate protein biosynthesis through a feedback mechanism. Whether a change in protein biosynthesis modulates protein degradation has not been reported. In this study, we found that inhibition of protein biosynthesis induced phosphorylation/activation of AKT and led to phosphorylation of AKT target substrates, including FoxO1, GSK3α/β, p70S6K, AS160, and the E3 ubiquitin ligase MDM2. Phosphorylation of ribosomal protein S6 was also modulated by inhibition of protein biosynthesis. The AKT phosphorylation/activation was mediated mainly through the PI3K pathway because it was blocked by the PI3K inhibitor LY294002. The activated AKT phosphorylated MDM2 at Ser166 and promoted degradation of the tumor suppressor p53. These findings suggest that inhibition of protein biosynthesis can alter degradation of some proteins through activation of AKT. This study reveals a novel regulation of protein degradation and calls for caution in blocking protein biosynthesis to study the half-life of proteins. Background: Whether a change in protein biosynthesis modulates protein degradation is unknown. Results: Inhibition of protein biosynthesis induces activation of AKT (protein kinase B), leading to activation of E3 ubiquitin ligase and thus degradation of its substrate proteins. Conclusion: Protein degradation is regulated by protein biosynthesis. Significance: This study reveals a novel regulation of protein degradation." @default.
• W2034231497 created "2016-06-24" @default.
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• W2034231497 date "2013-08-01" @default.
• W2034231497 modified "2023-10-12" @default.
• W2034231497 title "Inhibition of Protein Synthesis Alters Protein Degradation through Activation of Protein Kinase B (AKT)" @default.
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• W2034231497 doi "https://doi.org/10.1074/jbc.m112.445148" @default.
• W2034231497 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3745334" @default.
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