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USP22 deubiquitinates SIRT1. 33 / 35
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"Ubiquitin specific protease 22 (USP22) reduced Sirt1 ubiquitination and degradation and decreased FN and TGF-beta1 expression in GMCs under both basal and AGEs treated conditions."
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"Our previous study has already found that USP22 could deubiquitinate and stabilize Sirt1 in GMCs ( Lin et al., 2012 )."
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"As shown in the data in Fig. 3 B, USP22-FLAG rather than USP22–C185S-FLAG could reduce the Sirt1 ubiquitination level, indicating that the USP22 plasmids functioned normally in the EMT model."
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"USP22 can deubiquitinate and stabilize the expression of Sirt1."
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"Meanwhile, USP22 may also antagonize p53 transcriptional activation by deubiquitinating and stabilizing Sirt1 [14] ."
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"Our previous research has shown that USP22 deubiquitinates and stabilizes Sirt1 to alleviate fibrotic changes in GMCs under HG conditions ( Huang et al., 2015 )."
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"In addition, USP22 knockdown prevented c-MYC-mediated reduction of SIRT1 ubiquitination (XREF_FIG) and increase in SIRT1 expression (XREF_SUPPLEMENTARY)."
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"Third, since USP7 has key roles in the p53 tumor suppressor pathway through stabilization of p53 via increasing MDM2 [6, 52], while USP22 is reported to antagonize p53 transcriptional activation by deubiquitinating Sirt1 to suppress [34], we further investigated p53p53 the effect of USP22 and USP7 inhibition on the p53 pathway."
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"Ubiquitin-specific peptidase USP22 negatively regulates the STAT signaling pathway by deubiquitinating SIRT1."
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"Knockdown of USP22 reversed the deubiquitination of Sirt1 mediated by KLF3-AS1 (Fig. 4D)."
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"USP22 can deubiquitinate Sirt1 and enhance its stability through c-MYC-related network, leading to FLT3 tyrosine kinase inhibitors (TKIs) resistance in acute myeloid leukemia (AML)."
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"Recent studies have found that USP22 negatively regulates STAT signaling and p53 activation [9] by deubiquitinating Sirt1 [15,16] ."
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"USP22 negatively regulates STAT signaling by deubiquitinating SIRT1 in colon cancer cells [15] ."
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"USP22 negatively regulates STAT signaling by deubiquitinating SIRT1 [15] ."
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"Mechanistically, USP22 influences OS cell biology by deubiquitinating silent mating type information regulation 2 homolog-1 (SIRT1) ."
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"Conversely, knockdown of endogenous USP22 by small interfering RNA dramatically enhanced polyubiquitination of endogenous Sirt1 in HCT116 cells ( Figures 2 B and S2 A), and led to a decrease in Sirt1 [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"For example, Lin et al. (2012) proposed that USP22 can suppress TP53 transcriptional activation by deubiquitinating SIRT1 ."
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"USP22, a member of the deubiquitinase family, USP22-mediated deubiquitination can stabilize the expression of SIRT1."
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"Therefore, USP22 interacts with Sirt1 via its N terminus to suppress Sirt1 ubiquitination.To study the functional roles of Sirt1 ubiquitination, we mapped the ubiquitination sites in Sirt1 protein usi[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"The low level of Sirt1/5KR ubiquitination suggested either experimental background or few remaining lysines may still exist for Sirt1 ubiquitination.Since we demonstrated that USP22 deubiquitinates Si[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Given that SIRT1 is deubiquitinated by USP22 and stabilized at the protein level (Armour etal., 2013; Lin etal., 2012) and previous studies have reported that SIRT1 could negatively influence the chemosensitivity of HCC cells (Chen etal., 2012), our results supported the notion that USP22 increases SIRT1 protein levels in HCC cells."
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"Collectively, USP22 might deubiquitinate SIRT1 and subsequently activate the AKT pathway, increasing the expression of MRP1 to induce MDR in HCC cells."
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"Notably, overexpression of USP22 effectively decreased K29‐linked ubiquitination of SIRT1 (Figure 5I)."
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"Western blotting analysis further proved that the knockdown of USP22 dramatically attenuated CTRP9-induced Sirt1 de-ubiquitination ( Fig. 3 H)."
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"54 In addition, USP22 deubiquitinates SIRT1 and promotes multidrug resistance (MDR) by activating the SIRT1-AKT-MRP1 pathway."
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"We found that CTRP9 increased the expression of USP22, which triggered the de-ubiquitination of Sirt1 and promoted cell autophagy.In conclusion, the present study demonstrated that CTRP9 alleviated li[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"The nicotinamide adenine dinucleotide (NAD)-dependent protein deacetylase sirtuin-1 (Sirt 1) is specifically deubiquitinated by USP22, and this deubiquitination leads to the stabilization of the Sirt1-repressed tumor protein p53, affecting transcriptional and proapoptotic activities (Lin Z et al., 2012)."
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"In addition to histones, USP22 deubiquitinates TRF1, CCNB1, CCND1, and SIRT1, thereby regulating involvement in metabolism, cycling, and apoptosis."
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"These findings indicated that Sirt1 deubiquitination by USP22 overexpression could prevent p53 transcriptional activation, although this work had significant limitations."
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"USP22 also deubiquitinates Sirt1, a NAD-dependent histone deacetylase, which antagonizes p53 transcriptional activity to regulate cell-cycle progression and apoptosis [14] ."
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"USP22 affected the biological functions of OS cells by deubiquitinating SIRT1."
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"For instance, HULC can upregulate the expression of the ubiquitin specific peptidase 22 (USP22) protein by suppressing miR-6825-5p, miR-6845-5p, and miR-6886-3p at the epigenetic or transcriptional level in HCC cells; USP22 enhances the HULC induced deubiquitination of Sirt1 and stabilizes it, and Sirt1 stability induces the autophagy of HCC cells, thus increasing the resistance of HCC cells to oxaliplatin [XREF_BIBR]."
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"We have previously proven that USP22 could deubiquitinate and stabilize Sirt1 in GMCs, thereby regulating the pathological process of diabetic renal fibrosis ( Huang et al., 2015 ), indicating that US[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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