Affinage

USP22

Ubiquitin carboxyl-terminal hydrolase 22 · UniProt Q9UPT9

Length
525 aa
Mass
60.0 kDa
Annotated
2026-06-11
100 papers in source corpus 53 papers cited in narrative 53 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 9/9 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

USP22 is the catalytic deubiquitylase subunit of the human SAGA transcriptional coactivator complex, where it hydrolyzes monoubiquitin from histones H2B and H2A to control activated transcription, transcriptional elongation, mRNA 3'-end processing, and cell-cycle progression (PMID:18206973, PMID:18469533, PMID:22067483). Within SAGA, USP22 is recruited to target genes by activators such as Myc and engages SIRT1 through its ZnF-UBP domain; the recruited SIRT1 deacetylates SAGA components, and reciprocal acetylation of USP22 modulates how the deubiquitinase module docks onto the core complex (PMID:18206973, PMID:23382074). Through this chromatin activity, USP22 governs developmental programs—it is required for embryonic stem cell exit from self-renewal by hydrolyzing H2Bub at the Sox2 promoter, and Usp22 loss disrupts lineage specification in intestine and brain independent of bulk H2Bub1 levels (PMID:23760504, PMID:26431380). Beyond histones, USP22 is a multi-substrate deubiquitinase that stabilizes diverse non-histone proteins by removing degradative ubiquitin chains: it stabilizes SIRT1 to suppress p53-dependent apoptosis, an activity essential for embryonic viability (PMID:22542455), and the catalytic-site requirement for these functions is established by active-site mutants (C185S, Y513C) that abolish maintenance of substrate levels and cell-cycle control (PMID:26143114). Its substrate repertoire spans transcription factors and chromatin regulators (KDM1A/LSD1, c-Myc, PU.1, BMI1, E2F6, ZEB1, Snail1, PPARγ) (PMID:27501329, PMID:28160502, PMID:29844011, PMID:28415621, PMID:34339800, PMID:36906615, PMID:37001578, PMID:35449157), cell-cycle and growth-control proteins (CCND1, PTEN) (PMID:30224477, PMID:34743406), metabolic enzymes (FASN) (PMID:36333288), and receptors/signaling nodes (EGFR deubiquitinated on late endosomes, ERα, HIF1α) (PMID:29981430, PMID:32494025, PMID:31776228). In immunity and cell death, USP22 stabilizes KPNA2 to drive IRF3 nuclear translocation and type I interferon production, deubiquitinates RIPK3 to restrain necroptosis, stabilizes ATG5 to promote autophagic suppression of the NLRP3 inflammasome, stabilizes STAT1 to sustain IFNγ sensitivity, and stabilizes PD-L1 to dampen antitumor immunity (PMID:32130408, PMID:33369872, PMID:35900990, PMID:33601053, PMID:32665011). USP22 also promotes DNA double-strand break repair, facilitating BRCA2/PALB2/Rad51 recruitment for homologous recombination and supporting c-NHEJ during antibody class switch and V(D)J recombination (PMID:31685642, PMID:29520062). Across cancers USP22 exhibits context-dependent oncogenic and tumor-suppressive roles, suppressing mTOR signaling in the intestine while promoting proliferation, stemness, metabolic reprogramming, and therapy resistance elsewhere (PMID:31527800, PMID:30224477, PMID:31776228). USP22 transcription is itself regulated—repressed by an Sp1 site at its promoter and by p53—and small-molecule inhibitors (Rottlerin, Morusin, demethylzeylasteral) targeting residues including Leu475 and Arg419 reduce its substrate stabilization (PMID:23300749, PMID:36333288, PMID:37769523, PMID:39525573).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 2005 Medium

    Established that USP22 is a bona fide enzyme, defining it as a UBP-family deubiquitinase with the conserved catalytic residues required for ubiquitin hydrolysis.

    Evidence Sequence/domain analysis and biochemical DUB activity assay on the ~525 aa protein and its mouse homolog

    PMID:16378762

    Open questions at the time
    • No physiological substrate identified at this stage
    • No structural model of the catalytic domain
  2. 2008 High

    Placed USP22 within the SAGA coactivator complex and identified histones as its substrates, explaining how a DUB controls transcription and cell-cycle progression.

    Evidence Biochemical subunit purification, in vitro H2B and H2A deubiquitylation, ChIP, and RNAi loss-of-function

    PMID:18206973 PMID:18469533

    Open questions at the time
    • Relative contribution of H2B vs H2A deubiquitylation to specific genes unresolved
    • Mechanism of activator-directed recruitment beyond Myc not detailed
  3. 2011 Medium

    Extended USP22's chromatin role beyond histone removal to transcriptional elongation, 3'-end processing, and recruitment/stable loading of regulatory factors at target loci.

    Evidence RNAi knockdown, ChIP, qRT-PCR, and ubiquitination assays at IRF1 and p21 loci (FBP1)

    PMID:21779003 PMID:22067483

    Open questions at the time
    • Direct link between H2Bub and CPSF73/Pol II Ser2-P recruitment mechanistic detail incomplete
    • Generality across the genome not established
  4. 2012 High

    Demonstrated USP22 acts on non-histone substrates in vivo, showing SIRT1 stabilization suppresses p53 and is essential for embryonic viability—reframing USP22 as a multi-substrate DUB.

    Evidence Reciprocal Co-IP, ubiquitination assay, RNAi, and Usp22 knockout mouse

    PMID:22542455

    Open questions at the time
    • Whether SIRT1 stabilization is SAGA-dependent or cytoplasmic not fully resolved
    • Full breadth of non-histone substrate spectrum unknown at this point
  5. 2013 High

    Defined the structural basis of the USP22–SIRT1 interaction and showed reciprocal post-translational crosstalk (USP22 acetylation, SIRT1 deacetylation of SAGA) regulating DUB module assembly.

    Evidence Comparative Co-IP/MS interactome, ZnF-UBP domain mutagenesis, acetylation site mapping

    PMID:23382074

    Open questions at the time
    • Enzyme responsible for USP22 acetylation not identified
    • Functional consequence of K129 acetylation on substrate selection not quantified
  6. 2013 High

    Connected USP22 chromatin activity to a developmental decision, showing H2Bub removal at Sox2 represses pluripotency and licenses ESC differentiation.

    Evidence Knockdown/knockout in ESCs, ChIP, locus H2Bub analysis, three-germ-layer differentiation assays

    PMID:23760504

    Open questions at the time
    • Whether other pluripotency loci are co-regulated not addressed
    • Recruitment determinants at the Sox2 promoter undefined
  7. 2015 Medium

    Provided genetic active-site evidence directly tying USP22 catalytic activity to maintenance of cell-cycle regulators and demonstrated tissue-level differentiation roles uncoupled from bulk H2Bub1.

    Evidence C185S/Y513C active-site mutants with cell-cycle readout; Usp22 hypomorphic mouse with intestine/brain phenotypes and unchanged global H2Bub1

    PMID:26143114 PMID:26431380

    Open questions at the time
    • Locus-specific vs global H2Bub effects not reconciled
    • Which substrates dominate the differentiation phenotype unclear
  8. 2018 High

    Expanded USP22 into receptor and endosomal signaling and direct cell-cycle control, deubiquitinating EGFR on late endosomes to sustain signaling and stabilizing cyclin D1 independent of T286 phosphorylation.

    Evidence Co-IP, ubiquitination assays, endosomal localization, recycling assay, cycloheximide chase, cell-cycle analysis

    PMID:29981430 PMID:30224477

    Open questions at the time
    • How a SAGA subunit accesses late endosomal EGFR mechanistically unexplained
    • Cytoplasmic vs nuclear pools of USP22 not quantified
  9. 2018 High

    Established USP22's roles in DNA repair and hematopoietic differentiation through PU.1 stabilization and c-NHEJ facilitation, with in vivo genetic models.

    Evidence Conditional B-cell and Kras-progenitor knockouts, ubiquitylation assays, γH2AX/CSR/V(D)J readouts, PU.1 rescue

    PMID:29520062 PMID:29844011

    Open questions at the time
    • Direct DNA-repair substrate(s) underlying c-NHEJ effect not all defined
    • Tissue-context determinants of oncogenic vs differentiation roles unclear
  10. 2019 High

    Revealed USP22's context-dependent tumor biology—tumor-suppressive via mTOR restraint in intestine versus oncogenic stabilization of HIF1α—and demonstrated direct roles in homologous recombination repair.

    Evidence Tissue-specific conditional KO mice, mTOR pharmacological rescue, ubiquitination/ChIP assays for HIF1α, BRCA2/PALB2/Rad51 foci and HR reporter assays

    PMID:31527800 PMID:31685642 PMID:31776228

    Open questions at the time
    • Molecular determinant switching USP22 between suppressor and oncogene unknown
    • Whether HR function requires SAGA or is chromatin-independent unresolved
  11. 2020 High

    Positioned USP22 as a central regulator of innate immunity and cell death by stabilizing KPNA2 (IRF3 translocation/IFN-I), restraining RIPK3-driven necroptosis, and stabilizing PD-L1 and the iNKT transcriptional program.

    Evidence Co-IP, linkage-specific and remnant-profiling ubiquitination assays, RIPK3 site mutagenesis, conditional KO mice, viral and necroptosis models

    PMID:32069354 PMID:32130408 PMID:32665011 PMID:33369872

    Open questions at the time
    • How USP22 selects K-linkage-specific chains on different substrates unclear
    • Cytoplasmic targeting signals for these substrates undefined
  12. 2022 High

    Linked USP22 to metabolic and inflammatory homeostasis through site-specific stabilization of PPARγ, FASN, and ATG5, the latter coupling autophagy to NLRP3 inflammasome suppression.

    Evidence Co-IP, linkage- and lysine-site-specific ubiquitination assays, autophagy/lipogenesis assays, in vivo inflammation and tumor models

    PMID:35449157 PMID:35900990 PMID:36333288

    Open questions at the time
    • Determinants of site-specific deubiquitination (e.g. ATG5 Lys118) not structurally explained
    • Crosstalk between metabolic and immune substrates in vivo not integrated
  13. 2024 Medium

    Advanced USP22 as a druggable target, identifying selective small-molecule inhibitors and binding residues whose engagement reduces stabilization of substrates including PD-L1 and SIRT1.

    Evidence Structure-based virtual screening, in vitro enzyme assays, binding/MD studies, cellular ubiquitination assays, syngeneic and PDX tumor models

    PMID:37769523 PMID:39300073 PMID:39525573

    Open questions at the time
    • No experimentally determined high-resolution USP22 structure reported in the corpus
    • Selectivity over other USP-family DUBs only partially profiled

Open questions

Synthesis pass · forward-looking unresolved questions
  • It remains unresolved how a single SAGA-associated deubiquitinase achieves substrate selectivity across dozens of histone and non-histone targets and how cellular context dictates its opposing tumor-suppressive versus oncogenic outputs.
  • No unifying model for substrate/linkage discrimination
  • No high-resolution structure of full-length USP22 or its substrate complexes
  • Determinants of nuclear/SAGA vs cytoplasmic substrate engagement undefined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140096 catalytic activity, acting on a protein 8 GO:0140110 transcription regulator activity 5 GO:0016787 hydrolase activity 3
Localization
GO:0000228 nuclear chromosome 4 GO:0005634 nucleus 3 GO:0005829 cytosol 2 GO:0005768 endosome 1
Pathway
R-HSA-1643685 Disease 5 R-HSA-168256 Immune System 5 R-HSA-74160 Gene expression (Transcription) 4 R-HSA-1430728 Metabolism 3 R-HSA-4839726 Chromatin organization 3 R-HSA-73894 DNA Repair 3 R-HSA-1640170 Cell Cycle 2 R-HSA-5357801 Programmed Cell Death 2
Partners
BRCA2HIF1AKDM1AKPNA2PALB2PPARGRIPK3SIRT1
Complex memberships
SAGA/STAGA deubiquitinase module

Evidence

Reading pass · 53 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2008 USP22 is a catalytic subunit of the human SAGA (hSAGA) transcriptional cofactor complex where it deubiquitylates histone H2B. It is recruited to specific genes by activators such as Myc and is required for activated transcription and cell-cycle progression. Biochemical subunit identification, in vitro deubiquitylation assay, chromatin immunoprecipitation, RNAi loss-of-function Molecular cell High 18206973
2008 USP22 deubiquitylates histone H2A in addition to H2B, antagonizing Polycomb-catalyzed H2A ubiquitylation and thereby activating transcription. Biochemical substrate specificity assay with purified USP22 Cell cycle (Georgetown, Tex.) Medium 18469533
2005 USP22 (and its mouse homolog Usp22) encode ~525 aa proteins containing the conserved Cys, Asp(I), His, Asp/Asn(II) catalytic domains of the UBP deubiquitinase family and possess deubiquitinating enzyme activity in biochemical assay. Biochemical deubiquitinase activity assay, sequence/domain analysis Gene expression patterns : GEP Medium 16378762
2012 USP22 interacts with and deubiquitinates SIRT1, removing polyubiquitin chains and stabilizing SIRT1 protein. USP22-mediated SIRT1 stabilization suppresses p53 acetylation and p53-dependent apoptosis. Genetic deletion of Usp22 in mice causes SIRT1 instability, elevated p53 activity, and early embryonic lethality. Co-immunoprecipitation, ubiquitination assay, RNAi knockdown, genetic knockout mouse model Molecular cell High 22542455
2011 USP22 deubiquitinates the transcriptional regulator FBP1 (FUSE-binding protein 1); increased FBP1 polyubiquitination upon USP22 ablation does not alter FBP1 stability but reduces its stable recruitment to target loci (including the p21 gene), thereby regulating p21 expression and cell proliferation. RNAi knockdown, ubiquitination assay, chromatin immunoprecipitation EMBO reports Medium 21779003
2011 USP22 knockdown leads to increased monoubiquitination of histone H2B and impaired transcriptional elongation at the STAT1 target gene IRF1; USP22 depletion also diminishes 3'-end cleavage/polyadenylation and impairs recruitment of polyadenylation factor CPSF73 and serine 2 phosphorylation of RNA Pol II CTD. RNAi knockdown, ChIP, quantitative RT-PCR, rescue by overexpression FASEB journal Medium 22067483
2013 SIRT1 interacts with USP22 via the ZnF-UBP domain of USP22; this interaction is disrupted by the SIRT1 H363Y inactivating mutation. USP22 is acetylated on multiple lysines; acetylation of K129 within the ZnF-UBP domain alters interaction of the DUB module with the core SAGA complex. SIRT1 recruited by USP22 deacetylates individual SAGA complex components. High-confidence interactome mapping (comparative Co-IP/MS), domain mutagenesis, acetylation mapping Molecular and cellular biology High 23382074
2013 USP22 is required for embryonic stem cell differentiation into all three germ layers. USP22 occupies the Sox2 promoter and hydrolyzes monoubiquitin from H2B, repressing Sox2 transcription; this repression is required for ESCs to transition from self-renewal to differentiation. Loss-of-function (knockdown/knockout in ESCs), chromatin immunoprecipitation, differentiation assays, H2Bub analysis The Journal of biological chemistry High 23760504
2016 USP22 deubiquitylates and stabilizes the histone demethylase KDM1A (LSD1) after KDM1A is phosphorylated at Ser683 by GSK3β (primed by CK1α phosphorylation at Ser687). Phosphorylated KDM1A binds USP22, which removes ubiquitin and prevents its proteasomal degradation; this stabilization is required for H3K4 demethylation and repression of BMP2/CDKN1A/GATA6 to drive glioblastoma tumorigenesis. Co-immunoprecipitation, ubiquitination assay, phosphorylation mapping, mutagenesis, ChIP, xenograft models Nature cell biology High 27501329
2017 USP22 deubiquitinates c-Myc, preventing its proteasomal degradation and increasing c-Myc protein levels in breast cancer cells; USP22 knockdown reduces c-Myc levels. Co-immunoprecipitation, ubiquitination assay, knockdown/overexpression Journal of cellular physiology Medium 28160502
2018 USP22 directly deubiquitylates cyclin D1 (CCND1), protecting it from proteasome-mediated degradation through a mechanism distinct from canonical T286 phosphorylation-dependent ubiquitylation. This non-transcriptional control of CCND1 is a key mechanism by which USP22 promotes G1 cell cycle progression in cancer cells. Ubiquitylation assay, protein stability assay (cycloheximide chase), cell cycle analysis, cancer cell knockdown/KO Proceedings of the National Academy of Sciences of the United States of America High 30224477
2018 Usp22 (the mouse homolog) promotes antibody class switch recombination and V(D)J recombination by facilitating classical non-homologous end joining (c-NHEJ) for DNA break repair; Usp22 ablation in B cells impairs γH2AX formation and c-NHEJ. CSR to IgA is more reliant on alternative end joining and is less affected by Usp22 loss. Conditional knockout in primary B cells, γH2AX analysis, CSR/V(D)J recombination assays, epistasis with DNA repair pathways Nature communications High 29520062
2018 USP22 deficiency in the context of oncogenic Kras promotes AML transformation by blocking myeloid differentiation. USP22 functions as a deubiquitylase for PU.1, positively regulating PU.1 protein stability and the expression of PU.1 target genes; reconstitution of PU.1 in USP22-deficient Kras progenitors rescues differentiation. Conditional knockout mouse model, bone marrow transplantation, ubiquitylation assay, transcriptomic analysis, PU.1 rescue experiment Blood High 29844011
2019 USP22 deubiquitinates and stabilizes HIF1α, promoting hypoxia-induced HCC stemness and glycolysis. In TP53 wild-type cells, HIF1α-induced TP53 suppresses USP22 upregulation; in TP53-mutant cells, USP22 and HIF1α form a positive feedback loop. Immunoprecipitation, ubiquitination assay, chromatin immunoprecipitation, loss/gain-of-function, in vivo mouse model Gut High 31776228
2019 Loss of USP22 in murine intestinal epithelium exacerbates Apc-mutant intestinal tumor burden and increases mTOR activity; USP22 depletion in human CRC cells increases tumorigenic properties reversed by mTOR inhibitor treatment, indicating USP22 exerts tumor-suppressive function in colorectal cancer via mTOR suppression. Tissue-specific conditional knockout mouse model, in vivo tumor assays, mTOR pathway analysis, pharmacological rescue Cell death and differentiation High 31527800
2020 Cytoplasmic USP22 promotes nuclear translocation of IRF3 after viral infection by deubiquitinating and stabilizing the importin protein KPNA2. Viral infection induces USP22-IRF3 association in the cytoplasm in a KPNA2-dependent manner; USP22 or KPNA2 knockout impairs IRF3 nuclear translocation and type I IFN production. Reconstitution of KPNA2 into USP22-KO cells restores antiviral responses. Co-immunoprecipitation, ubiquitination assay, conditional knockout mice (Cre-ER and Lyz2-Cre), KPNA2 reconstitution epistasis, viral infection models The Journal of experimental medicine High 32130408
2020 USP22 deubiquitinates PD-L1 directly, inhibiting its proteasomal degradation and stabilizing PD-L1 protein. USP22 also deubiquitinates CSN5 and stabilizes it; either USP22 or CSN5 facilitates the interaction of PD-L1 with the other. USP22 removes K6, K11, K27, K29, K33, and K63-linked ubiquitin chains from both CSN5 and PD-L1. Co-immunoprecipitation, ubiquitination assay specifying linkage types, protein half-life assay, flow cytometry Cell communication and signaling : CCS Medium 32665011
2020 USP22 controls necroptosis by deubiquitinating RIPK3 at lysines 42, 351, and 518; mutation of RIPK3 K518 reduces necroptosis-associated ubiquitination and amplifies necrosome formation and necroptotic cell death. Loss of USP22 delays TNFα/Smac mimetic/zVAD-induced necroptosis without affecting NF-κB activation or extrinsic apoptosis. USP22 knockout in human tumor cell lines, ubiquitin remnant profiling (mass spectrometry), RIPK3 mutagenesis, cell death assays EMBO reports High 33369872
2020 USP22 interacts with MED1 (Mediator complex subunit 1) in iNKT cells. USP22 does not deubiquitinate MED1 for its stabilization; instead, USP22 enhances MED1 transcriptional activity for IL-2Rβ and T-bet gene expression through deubiquitination of histone H2A (not H2B). USP22 deficiency blocks iNKT cell development at stage 1→2 transition in a cell-intrinsic manner. Co-immunoprecipitation, H2A ubiquitination assay, conditional knockout mouse model, iNKT developmental analysis The Journal of experimental medicine High 32069354
2019 USP22 loss in murine placental endothelial cells and pericytes causes embryonic lethality due to defects in extra-embryonic placental vasculature; USP22 deletion hinders TGFβ and receptor tyrosine kinase signaling cascades with detrimental effects on cell survival, differentiation, and vessel formation. Conditional knockout mouse model, embryonic stem cell-derived endothelial/pericyte differentiation, signaling pathway analysis Development (Cambridge, England) Medium 30718289
2015 Global reduction of Usp22 in mice impairs lineage specification in the small intestine and brain, with altered frequencies of differentiated cells, while H2B and H2Bub1 levels remain constant, indicating USP22 controls differentiation through mechanisms beyond bulk H2Bub1 levels. Usp22 hypomorphic (lacZ knock-in) mouse model, histological analysis, H2Bub1 Western blot Oncotarget Medium 26431380
2022 USP22 directly interacts with, deubiquitinates (K48-linked), and stabilizes PPARγ, which in turn increases ACC and ACLY expression, promoting de novo fatty acid synthesis and HCC tumorigenesis. Co-immunoprecipitation, ubiquitination assay (K48-linkage specific), in vivo tumorigenesis experiments with PPARγ/ACLY/ACC inhibition Nature communications High 35449157
2022 USP22 stabilizes ATG5 by decreasing K27- and K48-linked ubiquitination at Lys118, thereby promoting ATG5-mediated autophagy, which in turn degrades NLRP3 and suppresses NLRP3 inflammasome activation. USP22 deficiency increases alum-induced peritonitis and LPS-induced systemic inflammation in vivo. Co-immunoprecipitation, site-specific ubiquitination assay (K27/K48 linkage, Lys118 mutagenesis), autophagy assays, in vivo USP22 silencing models Autophagy High 35900990
2022 USP22 controls basal and cGAMP-induced STING activation in human intestinal epithelial cells; loss of USP22 upregulates IFN-λ secretion and ISGs through STING, and USP22-deficient cells are protected against SARS-CoV-2 infection in a STING-dependent manner. USP22-deficient human intestinal epithelial cell lines, STING pathway analysis, SARS-CoV-2 infection assays, epistasis with STING inhibition Cell death & disease Medium 35933402
2019 USP22 interacts with and deubiquitinates BRCA2/PALB2, stabilizing their protein levels; this interaction occurs through the C-terminal WD40 domain of PALB2 and stimulates USP22 catalytic activity in vitro. USP22 is necessary for BRCA2, PALB2, and Rad51 recruitment to DNA double-strand breaks, facilitating homologous recombination repair. Co-immunoprecipitation, in vitro catalytic activity assay, DNA damage foci analysis, HR reporter assay Molecular cancer research : MCR Medium 31685642
2019 USP22 depletion in prostate cancer cells sensitizes them to genotoxic insult; ubiquitylome analysis identified XPC (nucleotide excision repair protein) as a USP22 substrate that undergoes deubiquitylation by USP22 to promote survival after DNA damage. Ubiquitylome profiling, USP22 KO/KD, genotoxic sensitivity assays, novel USP22-overexpressing murine model Cancer research Medium 31740444
2014 USP22 regulates androgen receptor (AR) accumulation and signaling; it is sufficient to reprogram AR function and induce transition to therapeutic resistance in prostate cancer xenograft models. Xenograft models, USP22 modulation (overexpression/depletion), AR signaling pathway analysis Cancer research Medium 24197134
2015 USP22 directly interacts with and deubiquitinates COX-2, modulating COX-2 stability; USP22 silencing decreases COX-2 protein half-life and inhibits lung carcinoma cell proliferation. Co-immunoprecipitation, ubiquitination assay, cycloheximide-chase protein stability assay Biochemical and biophysical research communications Medium 25817787
2018 USP22 deubiquitinates EGFR on late endosomes, preventing ubiquitin-mediated EGFR degradation and enhancing EGFR recycling after EGF stimulation, thereby sustaining EGFR downstream signaling (STAT3, AKT/mTOR, MEK/ERK) and conferring resistance to EGFR-TKIs. Co-immunoprecipitation, ubiquitination assay, endosomal localization, EGFR recycling assay, in vitro and in vivo knockdown Cancer letters Medium 29981430
2020 USP22 positively modulates ERα stability and transactivation via its deubiquitinase activity; USP22 is recruited together with ERα to cis-regulatory elements of ERα target genes, and USP22 deubiquitinase activity is required for maintaining ERα stability and conferring endocrine resistance. Co-immunoprecipitation, ChIP, ubiquitination assay, mutagenesis (deubiquitinase-dead), overexpression/knockdown Cell death and differentiation Medium 32494025
2014 USP22 promotes EMT in pancreatic cancer cells through the FAK signaling pathway, promoting Ezrin redistribution/phosphorylation, cytoskeletal remodeling, and upregulation of EMT transcription factors Snail and ZEB1; blockade of USP22 reverses these effects. Overexpression/knockdown in PANC-1 cells, phosphorylation analysis, immunofluorescence, invasion assay Oncology reports Low 25070659
2014 USP22 interacts with NFATc2 and deubiquitinates it, stabilizing NFATc2 protein levels; USP22 depletion in T cells reduces IL-2 expression, and this stabilization requires USP22 deubiquitinase activity. Co-immunoprecipitation, ubiquitination assay, knockdown in T cells, IL-2 expression analysis FEBS letters Medium 24561192
2014 USP22 overexpression downregulates STAT3 acetylation by deubiquitinating and stabilizing SIRT1; USP22, SIRT1, and STAT3 form a single protein complex. USP22 knockdown destabilizes SIRT1 and elevates STAT3 acetylation, with downstream reduction of MMP9 and TWIST expression. Co-immunoprecipitation, ubiquitination assay, Western blot for acetylated STAT3 Cellular physiology and biochemistry Medium 24969755
2015 USP22 deubiquitinase activity (demonstrated with C185S and Y513C mutants) is necessary for cell cycle regulation in HeLa cells and is required for maintaining BMI-1, c-Myc, cyclin D2, and p53 levels. Active-site mutagenesis (C185S catalytic dead, Y513C activity-reduced), cell cycle analysis, Western blot Gene Medium 26143114
2017 USP22 stabilizes BMI1 protein in gastric cancer cells through deubiquitination; USP22 knockdown suppresses cancer stem cell sphere formation, reduces CD133/SOX2/OCT4/NANOG expression, and these effects are rescued by TAT-BMI1 protein reconstitution. Knockdown/overexpression, protein stability assay, sphere formation assay, BMI1 reconstitution rescue Oncotarget Medium 28415621
2021 USP22 deubiquitinates STAT1 and improves its stability in melanoma cells; USP22 deficiency impairs sensitivity to IFNγ-JAK1-STAT1 signaling, reducing T cell-mediated killing; USP22 overexpression enhances tumor cell sensitivity to T cell killing. Co-immunoprecipitation, ubiquitination assay, CRISPR-Cas9 KO screen, in vitro and in vivo T cell killing assays Molecular therapy Medium 33601053
2021 USP22 promotes HER2-driven mammary carcinoma by stabilizing the ER chaperone HSPA5, actively suppressing unfolded protein response (UPR) induction; USP22 loss renders tumor cells more sensitive to apoptosis and ER-stress targeting therapies. Genetic mouse models, human HER2+ cell lines, transcriptome-wide gene expression analysis, HSPA5 stability assay Oncogene Medium 34007022
2021 USP22 deubiquitinates and stabilizes E2F6, which transcriptionally represses the phosphatase DUSP1, leading to AKT activation in HCC cells. Co-immunoprecipitation, ubiquitination assay, luciferase reporter, knockdown epistasis Cancer letters Medium 34339800
2021 USP22 deubiquitinates and stabilizes PTEN in pancreatic cancer cells; USP22-mediated PTEN stabilization induces p21 expression through PTEN interaction with ANKHD1, inhibiting ANKHD1 binding to the p21 promoter. Co-immunoprecipitation, ubiquitination assay, ChIP, overexpression/knockdown Molecular oncology Medium 34743406
2023 USP22 deubiquitinates and stabilizes the EMT transcription factor Snail1 in renal tubular epithelial cells, depending on its deubiquitinase activity, thereby promoting EMT and diabetic renal tubulointerstitial fibrosis. Co-immunoprecipitation, ubiquitination assay, deubiquitinase activity mutant, in vivo db/db mouse model European journal of pharmacology Medium 37001578
2023 USP22 acts as a co-activator of VEGFA transcription by maintaining ZEB1 stability via its deubiquitinase activity; USP22 is recruited to ZEB1-binding elements on the VEGFA promoter and alters H2Bub1 levels to enhance ZEB1-mediated VEGFA transcription. Co-immunoprecipitation, ubiquitination assay, ChIP, H2Bub1 chromatin analysis, knockdown/overexpression Cell death & disease Medium 36906615
2022 PRDM1 enhances USP22 transcription, and USP22 in turn reduces SPI1 (PU.1) protein degradation through deubiquitination, which enhances PD-L1 transcription in HCC cells, dampening antitumor immunity. Co-immunoprecipitation, ubiquitination assay, ChIP, gain-of-function in vivo models Nature communications Medium 36509766
2018 Gα12 stabilizes SIRT1 protein through transcriptional induction of USP22 via HIF-1α; USP22 in turn deubiquitinates and stabilizes SIRT1 to regulate mitochondrial respiration and hepatic lipid metabolism. cDNA microarray, Gna12-KO mouse model, lentiviral overexpression, protein stability assay The Journal of clinical investigation Medium 30300140
2015 USP22 interacts with RCAN1 (regulator of calcineurin 1) and promotes RCAN1 deubiquitination and protein stabilization, antagonizing FBW7, NEDD4-2, and β-TrCP E3 ligase actions on RCAN1. IFN-α treatment dissociates RCAN1 from USP22, triggering RCAN1 ubiquitination and degradation. Co-immunoprecipitation, ubiquitination assay, E3 ligase competition assay, IFN-α treatment Journal of cellular physiology Medium 25546086
2024 Phosphorylated MYH9 (Ser1943) recruits USP22 to deubiquitinate and stabilize HIF-1α in lenvatinib-resistant HCC, promoting cancer stemness. A CK2 inhibitor or USP22 inhibitor effectively reversed lenvatinib resistance in vivo and in vitro. Immunoprecipitation, mass spectrometry, ubiquitination assay, RNA-sequencing, patient-derived xenograft models Signal transduction and targeted therapy Medium 39300073
2022 EZH2 inhibition transcriptionally upregulates USP22, which in turn stabilizes PD-L1 via deubiquitination in colorectal cancer cells. Knockdown of USP22 enhances therapeutic efficacy of EZH2 inhibitors. USP22 knockdown/overexpression, ubiquitination assay, protein stability assay, in vivo tumor models Advanced science (Weinheim, Baden-Wurttemberg, Germany) Medium 38520088
2024 The small molecule demethylzeylasteral (Dem) binds USP22 and promotes its degradation, resulting in increased ubiquitination and proteasomal degradation of PD-L1; structure-based analysis identified Leu475 and Arg419 as crucial residues for USP22 inhibitor binding. Structure-based virtual screening, binding assay, ubiquitination assay, in vivo syngeneic tumor model, molecular dynamics simulation Acta pharmaceutica Sinica. B Medium 39525573
2023 Structure-based inhibitor discovery identified Rottlerin and Morusin as selective USP22 inhibitors (IC50 2.53 and 8.29 μM, respectively); treatment with these compounds increases H2A and H2B monoubiquitination and reduces Sirt1 and PD-L1 protein levels, consistent with USP22 substrate specificity. Key binding residues Leu475 (conserved) and Arg419 (non-conserved) are crucial for inhibitory function. Structure-based virtual screening, in vitro USP22 enzyme assay, cellular ubiquitination assay, in vivo syngeneic tumor model, molecular dynamics/binding free energy calculation Bioorganic chemistry Medium 37769523
2012 The USP22 promoter basal activity is controlled by the -210 to -7 region; an Sp1 binding site immediately upstream of the transcriptional start site (-13 to -7) acts as a repressor—Sp1 binding suppresses USP22 transcription, and Sp1 knockdown or inhibition increases USP22 mRNA levels. 5'-RACE, promoter deletion analysis, mutagenesis, Sp1 ChIP, mithramycin A treatment, Sp1 overexpression/knockdown PloS one Medium 23300749
2020 USP22 depletion in pancreatic tumor cells reduces myeloid cell infiltration and promotes T cell and NK cell infiltration, leading to improved response to combination immunotherapy; USP22 exerts its effects on the tumor immune microenvironment through its association with the deubiquitylase module of the SAGA/STAGA complex and reshaping the cancer cell transcriptome. USP22 deletion in pancreatic tumor cells, immune cell profiling, immunotherapy response assay, SAGA complex association analysis Cancer immunology research Medium 31871120
2021 USP22 suppresses SPARC expression in intestinal epithelial cells by affecting H3K27ac and H2Bub1 occupancy on the SPARC gene; Usp22 intestine-specific deletion upregulates SPARC and increases colitis severity and inflammation-associated colorectal tumor growth. Intestine-specific conditional Usp22 KO mouse, DSS colitis model, chromatin immunoprecipitation (H3K27ac, H2Bub1), gene expression analysis Cancers Medium 33920268
2022 USP22 deubiquitinates and stabilizes FASN; in p53 wild-type CRC cells, H2O2-induced p53 represses USP22 transcription, reducing FASN stability and fatty acid synthesis. In p53-deficient cells, this repression is relieved, leading to FASN stabilization and increased lipid synthesis. Co-immunoprecipitation, ubiquitination assay, FASN protein stability assay, p53 transcriptional repression of USP22, lipogenesis assay Cell death discovery Medium 36333288
2021 USP22 deubiquitinates and stabilizes LSD1 (KDM1A) in osteosarcoma; USP22 knockdown leads to ubiquitination and degradation of LSD1, reduced p21 repression, and inhibited cell proliferation/invasion. miR-140 suppresses this axis by targeting USP22. Knockdown/overexpression, ubiquitination assay, protein stability assay, in vivo xenograft Molecular therapy. Nucleic acids Medium 33868787

Source papers

Stage 0 corpus · 100 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2008 The putative cancer stem cell marker USP22 is a subunit of the human SAGA complex required for activated transcription and cell-cycle progression. Molecular cell 359 18206973
2012 USP22 antagonizes p53 transcriptional activation by deubiquitinating Sirt1 to suppress cell apoptosis and is required for mouse embryonic development. Molecular cell 265 22542455
2020 USP22 Protects Against Myocardial Ischemia-Reperfusion Injury via the SIRT1-p53/SLC7A11-Dependent Inhibition of Ferroptosis-Induced Cardiomyocyte Death. Frontiers in physiology 178 33192549
2019 USP22 promotes hypoxia-induced hepatocellular carcinoma stemness by a HIF1α/USP22 positive feedback loop upon TP53 inactivation. Gut 168 31776228
2022 USP22 regulates lipidome accumulation by stabilizing PPARγ in hepatocellular carcinoma. Nature communications 165 35449157
2016 Nuclear GSK3β promotes tumorigenesis by phosphorylating KDM1A and inducing its deubiquitylation by USP22. Nature cell biology 145 27501329
2017 Deubiquitinating enzyme USP22 positively regulates c-Myc stability and tumorigenic activity in mammalian and breast cancer cells. Journal of cellular physiology 126 28160502
2008 USP22, an hSAGA subunit and potential cancer stem cell marker, reverses the polycomb-catalyzed ubiquitylation of histone H2A. Cell cycle (Georgetown, Tex.) 124 18469533
2011 USP22 regulates cell proliferation by deubiquitinating the transcriptional regulator FBP1. EMBO reports 118 21779003
2020 The deubiquitinase USP22 regulates PD-L1 degradation in human cancer cells. Cell communication and signaling : CCS 107 32665011
2018 Control of CCND1 ubiquitylation by the catalytic SAGA subunit USP22 is essential for cell cycle progression through G1 in cancer cells. Proceedings of the National Academy of Sciences of the United States of America 107 30224477
2013 USP22 regulates oncogenic signaling pathways to drive lethal cancer progression. Cancer research 104 24197134
2022 PRDM1/BLIMP1 induces cancer immune evasion by modulating the USP22-SPI1-PD-L1 axis in hepatocellular carcinoma cells. Nature communications 99 36509766
2017 USP22 mediates the multidrug resistance of hepatocellular carcinoma via the SIRT1/AKT/MRP1 signaling pathway. Molecular oncology 94 28417539
2021 LncRNA KCNQ1OT1 Secreted by Tumor Cell-Derived Exosomes Mediates Immune Escape in Colorectal Cancer by Regulating PD-L1 Ubiquitination via MiR-30a-5p/USP22. Frontiers in cell and developmental biology 81 34350172
2005 The expression patterns of deubiquitinating enzymes, USP22 and Usp22. Gene expression patterns : GEP 80 16378762
2012 USP22 acts as an oncogene by the activation of BMI-1-mediated INK4a/ARF pathway and Akt pathway. Cell biochemistry and biophysics 74 21928107
2013 The epigenetic modifier ubiquitin-specific protease 22 (USP22) regulates embryonic stem cell differentiation via transcriptional repression of sex-determining region Y-box 2 (SOX2). The Journal of biological chemistry 71 23760504
2022 USP22 suppresses the NLRP3 inflammasome by degrading NLRP3 via ATG5-dependent autophagy. Autophagy 69 35900990
2020 USP22 promotes IRF3 nuclear translocation and antiviral responses by deubiquitinating the importin protein KPNA2. The Journal of experimental medicine 69 32130408
2020 USP22 controls necroptosis by regulating receptor-interacting protein kinase 3 ubiquitination. EMBO reports 66 33369872
2018 MiR-30-5p suppresses cell chemoresistance and stemness in colorectal cancer through USP22/Wnt/β-catenin signaling axis. Journal of cellular and molecular medicine 66 30338942
2012 Expression patterns of USP22 and potential targets BMI-1, PTEN, p-AKT in non-small-cell lung cancer. Lung cancer (Amsterdam, Netherlands) 66 22717106
2018 MicroRNA-29c Increases the Chemosensitivity of Pancreatic Cancer Cells by Inhibiting USP22 Mediated Autophagy. Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology 65 29807360
2023 Bone marrow mesenchymal stem cell-derived exosomal lncRNA KLF3-AS1 stabilizes Sirt1 protein to improve cerebral ischemia/reperfusion injury via miR-206/USP22 axis. Molecular medicine (Cambridge, Mass.) 64 36627572
2017 MicroRNA-30e-5p suppresses non-small cell lung cancer tumorigenesis by regulating USP22-mediated Sirt1/JAK/STAT3 signaling. Experimental cell research 64 29174979
2022 Immune Evasion and Drug Resistance Mediated by USP22 in Cancer: Novel Targets and Mechanisms. Frontiers in immunology 63 35935969
2019 Oncogenic USP22 supports gastric cancer growth and metastasis by activating c-Myc/NAMPT/SIRT1-dependent FOXO1 and YAP signaling. Aging 63 31689236
2011 The co-expression of USP22 and BMI-1 may promote cancer progression and predict therapy failure in gastric carcinoma. Cell biochemistry and biophysics 63 21735131
2019 Tumor Cell-Intrinsic USP22 Suppresses Antitumor Immunity in Pancreatic Cancer. Cancer immunology research 61 31871120
2010 Silencing USP22 by asymmetric structure of interfering RNA inhibits proliferation and induces cell cycle arrest in bladder cancer cells. Molecular and cellular biochemistry 60 20824490
2018 The H2B deubiquitinase Usp22 promotes antibody class switch recombination by facilitating non-homologous end joining. Nature communications 57 29520062
2019 USP22 exerts tumor-suppressive functions in colorectal cancer by decreasing mTOR activity. Cell death and differentiation 55 31527800
2018 USP22 deficiency leads to myeloid leukemia upon oncogenic Kras activation through a PU.1-dependent mechanism. Blood 55 29844011
2013 A high-confidence interaction map identifies SIRT1 as a mediator of acetylation of USP22 and the SAGA coactivator complex. Molecular and cellular biology 55 23382074
2019 USP22 Functions as an Oncogenic Driver in Prostate Cancer by Regulating Cell Proliferation and DNA Repair. Cancer research 54 31740444
2018 Gα12 ablation exacerbates liver steatosis and obesity by suppressing USP22/SIRT1-regulated mitochondrial respiration. The Journal of clinical investigation 54 30300140
2017 USP22 Induces Cisplatin Resistance in Lung Adenocarcinoma by Regulating γH2AX-Mediated DNA Damage Repair and Ku70/Bax-Mediated Apoptosis. Frontiers in pharmacology 54 28567015
2021 Self-Activated Cascade-Responsive Sorafenib and USP22 shRNA Co-Delivery System for Synergetic Hepatocellular Carcinoma Therapy. Advanced science (Weinheim, Baden-Wurttemberg, Germany) 53 33717848
2018 USP22 promotes resistance to EGFR-TKIs by preventing ubiquitination-mediated EGFR degradation in EGFR-mutant lung adenocarcinoma. Cancer letters 52 29981430
2024 EZH2 Inhibition Enhances PD-L1 Protein Stability Through USP22-Mediated Deubiquitination in Colorectal Cancer. Advanced science (Weinheim, Baden-Wurttemberg, Germany) 51 38520088
2024 The p-MYH9/USP22/HIF-1α axis promotes lenvatinib resistance and cancer stemness in hepatocellular carcinoma. Signal transduction and targeted therapy 45 39300073
2015 USP22 promotes tumor progression and induces epithelial-mesenchymal transition in lung adenocarcinoma. Lung cancer (Amsterdam, Netherlands) 43 25907317
2019 USP22-dependent HSP90AB1 expression promotes resistance to HSP90 inhibition in mammary and colorectal cancer. Cell death & disease 39 31801945
2020 USP22 positively modulates ERα action via its deubiquitinase activity in breast cancer. Cell death and differentiation 38 32494025
2014 Ubiquitin-specific peptidase USP22 negatively regulates the STAT signaling pathway by deubiquitinating SIRT1. Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology 38 24969755
2014 USP22 promotes epithelial-mesenchymal transition via the FAK pathway in pancreatic cancer cells. Oncology reports 38 25070659
2017 USP22 maintains gastric cancer stem cell stemness and promotes gastric cancer progression by stabilizing BMI1 protein. Oncotarget 37 28415621
2016 Silencing of USP22 suppresses high glucose-induced apoptosis, ROS production and inflammation in podocytes. Molecular bioSystems 36 26953552
2019 USP22 controls multiple signaling pathways that are essential for vasculature formation in the mouse placenta. Development (Cambridge, England) 35 30718289
2012 USP22 nuclear expression is significantly associated with progression and unfavorable clinical outcome in human esophageal squamous cell carcinoma. Journal of cancer research and clinical oncology 35 22447106
2014 USP22 promotes NSCLC tumorigenesis via MDMX up-regulation and subsequent p53 inhibition. International journal of molecular sciences 34 25547493
2010 Implication of USP22 in the regulation of BMI-1, c-Myc, p16INK4a, p14ARF, and cyclin D2 expression in primary colorectal carcinomas. Diagnostic molecular pathology : the American journal of surgical pathology, part B 33 21052002
2020 RETRACTED: BMSCs-derived exosomal microRNA-let-7a plays a protective role in diabetic nephropathy via inhibition of USP22 expression. Life sciences 32 33347877
2018 Targeting USP22 Suppresses Tumorigenicity and Enhances Cisplatin Sensitivity Through ALDH1A3 Downregulation in Cancer-Initiating Cells from Lung Adenocarcinoma. Molecular cancer research : MCR 32 29720480
2013 RNA interference-mediated USP22 gene silencing promotes human brain glioma apoptosis and induces cell cycle arrest. Oncology letters 32 23599781
2017 USP22 drives colorectal cancer invasion and metastasis via epithelial-mesenchymal transition by activating AP4. Oncotarget 31 28427243
2015 USP22 acts as an oncogene by regulating the stability of cyclooxygenase-2 in non-small cell lung cancer. Biochemical and biophysical research communications 31 25817787
2011 The ubiquitin hydrolase USP22 contributes to 3'-end processing of JAK-STAT-inducible genes. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 31 22067483
2022 Upregulation of USP22 and ABCC1 during Sorafenib Treatment of Hepatocellular Carcinoma Contribute to Development of Resistance. Cells 30 35203285
2022 LncRNA MALAT1 Regulates USP22 Expression Through EZH2-Mediated H3K27me3 Modification to Accentuate Sepsis-Induced Myocardial Dysfunction. Cardiovascular toxicology 30 35726125
2021 USP22 promotes HER2-driven mammary carcinoma aggressiveness by suppressing the unfolded protein response. Oncogene 30 34007022
2021 ZRANB1 enhances stem-cell-like features and accelerates tumor progression by regulating Sox9-mediated USP22/Wnt/β-catenin pathway in colorectal cancer. Cellular signalling 30 34798260
2017 USP22 knockdown enhanced chemosensitivity of hepatocellular carcinoma cells to 5-Fu by up-regulation of Smad4 and suppression of Akt. Oncotarget 30 28445968
2015 Expression of USP22 and Survivin is an indicator of malignant behavior in hepatocellular carcinoma. International journal of oncology 30 26497847
2024 Demethylzeylasteral induces PD-L1 ubiquitin-proteasome degradation and promotes antitumor immunity via targeting USP22. Acta pharmaceutica Sinica. B 29 39525573
2020 USP22 promotes development of lung adenocarcinoma through ubiquitination and immunosuppression. Aging 27 32294625
2020 The USP22 promotes the growth of cancer cells through the DYRK1A in pancreatic ductal adenocarcinoma. Gene 27 32687947
2022 Targeting ferroptosis with miR-144-3p to attenuate pancreatic β cells dysfunction via regulating USP22/SIRT1 in type 2 diabetes. Diabetology & metabolic syndrome 26 35761309
2015 Usp22 deficiency impairs intestinal epithelial lineage specification in vivo. Oncotarget 26 26431380
2020 MiR-329-3p inhibits hepatocellular carcinoma cell proliferation and migration through USP22-Wnt/β-Catenin pathway. European review for medical and pharmacological sciences 25 33090397
2014 USP22 is a positive regulator of NFATc2 on promoting IL2 expression. FEBS letters 25 24561192
2022 Long Intergenic Noncoding RNA00265 Enhances Cell Viability and Metastasis via Targeting miR-485-5p/USP22 Axis in Osteosarcoma. Frontiers in oncology 24 35692754
2021 USP22 deficiency in melanoma mediates resistance to T cells through IFNγ-JAK1-STAT1 signal axis. Molecular therapy : the journal of the American Society of Gene Therapy 24 33601053
2018 MiR-30e-5p inhibits proliferation and metastasis of nasopharyngeal carcinoma cells by target-ing USP22. European review for medical and pharmacological sciences 24 30338802
2020 USP22 controls iNKT immunity through MED1 suppression of histone H2A monoubiquitination. The Journal of experimental medicine 23 32069354
2020 Long Non-Coding RNA SNHG16 Activates USP22 Expression to Promote Colorectal Cancer Progression by Sponging miR-132-3p. OncoTargets and therapy 23 32547062
2016 MiR-101 targets USP22 to inhibit the tumorigenesis of papillary thyroid carcinoma. American journal of cancer research 23 27904772
2021 USP22-mediated deubiquitination of PTEN inhibits pancreatic cancer progression by inducing p21 expression. Molecular oncology 22 34743406
2024 Hypoxic adipose stem cell-derived exosomes carrying high-abundant USP22 facilitate cutaneous wound healing through stabilizing HIF-1α and upregulating lncRNA H19. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 21 38738548
2021 miR-140 inhibits osteosarcoma progression by impairing USP22-mediated LSD1 stabilization and promoting p21 expression. Molecular therapy. Nucleic acids 21 33868787
2019 USP22 Interacts with PALB2 and Promotes Chemotherapy Resistance via Homologous Recombination of DNA Double-Strand Breaks. Molecular cancer research : MCR 21 31685642
2021 Deubiquitination of the repressor E2F6 by USP22 facilitates AKT activation and tumor growth in hepatocellular carcinoma. Cancer letters 20 34339800
2020 Hypoxia-induced USP22-BMI1 axis promotes the stemness and malignancy of glioma stem cells via regulation of HIF-1α. Life sciences 20 32070708
2023 USP22 upregulates ZEB1-mediated VEGFA transcription in hepatocellular carcinoma. Cell death & disease 19 36906615
2022 USP22 controls type III interferon signaling and SARS-CoV-2 infection through activation of STING. Cell death & disease 18 35933402
2021 USP22 Suppresses SPARC Expression in Acute Colitis and Inflammation-Associated Colorectal Cancer. Cancers 18 33920268
2023 USP22 aggravated diabetic renal tubulointerstitial fibrosis progression through deubiquitinating and stabilizing Snail1. European journal of pharmacology 17 37001578
2020 RNF220 promotes the proliferation of leukaemic cells and reduces the degradation of the Cyclin D1 protein through USP22. Blood cells, molecules & diseases 17 32896826
2017 USP22 down-regulation facilitates human retinoblastoma cell aging and apoptosis via inhibiting TERT/P53 pathway. European review for medical and pharmacological sciences 16 28682440
2012 Knock-down of USP22 by small interfering RNA interference inhibits HepG2 cell proliferation and induces cell cycle arrest. Cellular and molecular biology (Noisy-le-Grand, France) 16 23217440
2023 Discovery of selective and potent USP22 inhibitors via structure-based virtual screening and bioassays exerting anti-tumor activity. Bioorganic chemistry 15 37769523
2022 USP22 Contributes to Chemoresistance, Stemness, and EMT Phenotype of Triple-Negative Breast Cancer Cells by egulating the Warburg Effect via c-Myc Deubiquitination. Clinical breast cancer 15 36528490
2015 The deubiquitinating enzyme activity of USP22 is necessary for regulating HeLa cell growth. Gene 15 26143114
2012 Cloning and characterization of the human USP22 gene promoter. PloS one 15 23300749
2023 RNF220 promotes gastric cancer growth and stemness via modulating the USP22/wnt/β-catenin pathway. Tissue & cell 14 37295272
2022 Derepression of the USP22-FASN axis by p53 loss under oxidative stress drives lipogenesis and tumorigenesis. Cell death discovery 14 36333288
2021 USP22 promotes melanoma and BRAF inhibitor resistance via YAP stabilization. Oncology letters 13 33777217
2020 The POU2F1/miR-4490/USP22 axis regulates cell proliferation and metastasis in gastric cancer. Cellular oncology (Dordrecht, Netherlands) 13 32857323
2015 Ubiquitin-specific protease 22 (USP22) positively regulates RCAN1 protein levels through RCAN1 de-ubiquitination. Journal of cellular physiology 13 25546086

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