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USP22 activates SIRT1. 22 / 23
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"Collectively, these results revealed that CTRP9 promoted USP22 expression, which removed the conjugated poly-ubiquitin chains from Sirt1 and enhanced the stabilization of Sirt1 protein.As shown in Fig[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"The lncRNA highly upregulated in liver cancer ( HULC ) enhances expression of ubiquitin-specific peptidase (USP22) which increases stability of Sirt1 protein."
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"We found that USP22 promotes multidrug resistance in HCC cells by activating SIRT1/protein kinase B (Akt)/multidrug resistance-associated protein 1 (MRP1) pathway, while inhibition of USP22 and SIRT1 [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Simply put, USP22 may activate the SIRT1–AKT–MRP1 pathway and consequently promote MDR in human HCC cells (226)."
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"USP22 positively regulates the histone deacetylase Sirt1, resulting in suppression of p53 function by reducing p53 acetylation [58] ."
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"USP22 mediates stabilization of Sirt1 by interacting and removing poly-ubiquitin chains previously conjugated to Sirt1."
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"In our study, after treatment with FO, the expression of USP22 was markedly increased, and the increase in USP22 increased the activity of Sirt1 and decreased myocardial cell death."
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"Our data showed that USP22 overexpression increased the stability of SIRT1, thereby prolonging the half-life of SIRT1 protein (Fig. 4C)."
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"Furthermore, c-Myc-induced upregulation of USP22 deubiquitinase promotes SIRT1 stability and subsequently confers protection against FLT3 inhibitors in FLT3-ITD AML LSCs [136]."
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"In fact, expression of USP22 significantly prolonged the half-life of Sirt1 ( Figures 3 A and 3B )."
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"Because USP22 inhibits the ubiquitination-mediated Sirt1 degradation, we hypothesized that USP22 inhibits p53 functions through Sirt1."
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"This destabilization of Sirt1 protein caused by USP22 deficency results in elevated p53 acetylation ( Figures 6 F and S4 C) and target gene transcription because a significant increase in both protein[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"As BAX, p21, and Puma are de novo target genes of p53, our data collectively demonstrate that USP22 is required to enhance Sirt1-mediated suppression of p53 transcriptional activity and suppression of[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Especially, upregulation of USP22 can remove the conjugated ubiquitin chain of Sirt1, therefore reducing the degradation of Sirt1 protein mediated by ubiquitin in hepatocellular carcinoma (Xiong et al. 2017); A previous study has revealed that USP22-mediated Sirt1 signaling is involved in the tumorigenesis (Xu et al. 2018); Moreover, the binding sites of miR-206 with USP22 have been forecasted by bioinformatics."
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"Because treatment with siRNA for USP22 diminished G protein α12–induced accumulation of Sirt-1 in HepG2 cells, it was concluded that UPS22 stabilizes Sirt-1 [195]."
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"Additionally, after MIRI, the downregulation of USP22 induces the destabilization of SIRT1 via its deubiquitinase activity, leading to p53 upregulation accompanied by a decrease in SLC7A11 expression levels."
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"The transfection of SIRT1 OE or sh-USP22 successfully overexpressed SIRT1 or silenced USP22 in INS-1 cells (Fig. 4D, E)."
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"Our data revealed that knockdown of USP22 decreased the expression of stemness related genes Sox2 and CD133, redox related genes Nrf2 and Sirt1, and quiescence related genes PP2A and c-Myc in GSCs und[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"USP22 also increases SIRT1 protein stability, which leads to the suppression of p53 transcriptional activity and inhibition of cell death [XREF_BIBR, XREF_BIBR]."
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"As presented in Fig. 2 A–B , knockdown of USP22 inhibited the expression of stemness related genes Sox2 and CD133, redox related genes Nrf2 and Sirt1, and quiescence related genes PP2A and c-Myc."
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"Another protein involved in this track is ubiquitin-specific peptidase 22 (USP22), which mediates SIRT1 stability and its expression."
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"Moreover, silencing of USP22 reversed the promoted deubiquitinating of Sirt1 protein caused by overexpression of KLF3-AS1."
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