| 2010 |
OTUB1 suppresses RNF168-dependent K63-linked poly-ubiquitination at DNA double-strand breaks independently of its catalytic deubiquitinase activity by binding to and inhibiting UBC13 (UBE2N), the cognate E2 enzyme for RNF168. OTUB1 also binds E2s of the UBE2D and UBE2E subfamilies through the same non-canonical mechanism. |
Co-immunoprecipitation, in vitro ubiquitination assays, siRNA knockdown with DSB repair readouts, catalytic mutant analysis |
Nature |
High |
20725033
|
| 2012 |
Crystal structures of OTUB1–UBC13 and OTUB1 bound to ubiquitin aldehyde plus a chemical UBC13~Ub conjugate reveal that free ubiquitin allosterically binds a distal site on OTUB1, triggering conformational changes that form an N-terminal ubiquitin-binding helix, increase affinity for donor ubiquitin in the E2~Ub thiolester, occlude the RING E3 binding site on UBC13, and block acceptor-ubiquitin attack on the thiolester—thereby inhibiting K63-linked ubiquitin chain synthesis. |
X-ray crystallography, biochemical ubiquitination assays, structure-guided mutagenesis, surface plasmon resonance |
Nature |
High |
22367539
|
| 2012 |
OTUB1 co-opts its canonical Lys48-linked distal ubiquitin-binding site to recognize charged E2~Ub thioester intermediates; free ubiquitin binding at this site promotes formation of the inhibited E2 complex, with the donor-ubiquitin Lys48 positioned near the OTUB1 catalytic site in a configuration mimicking K48-linked chain cleavage products. |
X-ray crystallography, biochemical E2 inhibition assays, mutagenesis, structural analysis |
Molecular cell |
High |
22325355
|
| 2012 |
Crystal structure of human OTUB1 in complex with UBC13 and MMS2 at 3.15 Å resolution reveals atomic-level contacts required for inhibition of K63-linked ubiquitin chain formation; structure-based OTUB1 mutants fail to inhibit K63 chain formation in vitro and histone ubiquitination and 53BP1 foci in vivo. |
X-ray crystallography, surface plasmon resonance, structure-guided mutagenesis, in vitro ubiquitination assays, cell-based 53BP1 foci assay |
The Journal of biological chemistry |
High |
22679021
|
| 2013 |
E2 ubiquitin-conjugating enzymes (UBC13, UBCH5) stimulate OTUB1 catalytic cleavage of K48-linked polyubiquitin by stabilizing folding of the OTUB1 N-terminal ubiquitin-binding helix; this stimulation is regulated by the ratio of charged to uncharged E2 and by concentrations of K48 polyubiquitin and free ubiquitin, establishing bidirectional cross-regulation between OTUB1 and its E2 partners. |
Biochemical DUB activity assays, X-ray crystallography of human and worm OTUB1/UBCH5B, mutagenesis |
Nature structural & molecular biology |
High |
23955022
|
| 2009 |
OTUB1 interacts with TRAF3 and TRAF6 by co-immunoprecipitation and mediates their deubiquitination, thereby negatively regulating virus-triggered type I interferon induction and IRF3/NF-κB activation. |
Co-immunoprecipitation, overexpression/knockdown with reporter assays for IFN-β transcription, antiviral response assays |
The Journal of biological chemistry |
Medium |
19996094
|
| 2009 |
OTUB1 directly deubiquitinates estrogen receptor alpha (ERα) in vitro and in cells; it interacts with ERα (identified by mass spectrometry of an ERα complex) and negatively regulates ERα-mediated transcription while stabilizing ERα protein on chromatin. |
Mass spectrometry of ERα complex, in vitro deubiquitination assay, Co-IP, transcriptional reporter assays, ChIP |
The Journal of biological chemistry |
Medium |
19383985
|
| 2013 |
OTUB1 is recruited to the active phospho-SMAD2/3 complex upon TGFβ stimulation; it inhibits ubiquitylation and proteasomal degradation of phospho-SMAD2/3 via non-catalytic E2 inhibition (independent of its isopeptidase activity), thereby sustaining TGFβ-mediated gene transcription and cell migration. Depletion of OTUB1 causes rapid loss of phospho-SMAD2/3 rescued by the proteasomal inhibitor bortezomib. |
Co-immunoprecipitation (signal-dependent), siRNA knockdown, catalytic mutant analysis, proteasome inhibitor rescue, TGFβ reporter assays, migration assays |
Nature communications |
High |
24071738
|
| 2013 |
OTUB1 associates with c-IAP1 within the TWEAK receptor signalling complex, disassembles K48-linked polyubiquitin chains from c-IAP1 in vitro and in vivo, stabilises c-IAP1, and thereby sustains TWEAK-induced canonical NF-κB and MAPK signalling while preventing caspase activation and cell death. |
Co-immunoprecipitation, in vitro and in vivo deubiquitination assays, siRNA knockdown with caspase/NF-κB readouts, zebrafish c-IAP knockdown model |
The EMBO journal |
High |
23524849
|
| 2014 |
Otub1 suppresses MDM2-mediated p53 ubiquitination and stabilises p53 independently of its deubiquitinase activity by non-canonically inhibiting the E2 enzyme UbcH5; monoubiquitination of Otub1 (primarily at Lys59 and Lys109 by UbcH5) is required for Otub1 to suppress UbcH5 and stabilise p53, as a lysine-free Otub1 mutant (K0) fails to achieve these functions. |
In vitro ubiquitination/monoubiquitination assays, Co-IP, cycloheximide chase, apoptosis assays, cell proliferation assays, UbcH5 binding studies |
The Journal of biological chemistry |
High |
24403071
|
| 2015 |
Casein kinase 2 (CK2) phosphorylates OTUB1 at Ser16, promoting its nuclear accumulation; pharmacological CK2 inhibition or genetic ablation blocks Ser16 phosphorylation and causes nuclear exclusion of OTUB1. Ser16-phosphorylated OTUB1 is detected exclusively in the nucleus and promotes 53BP1 DNA repair foci formation after ionising radiation. |
In vitro CK2 phosphorylation assay, phospho-specific antibody, CK2 inhibitor/KO, subcellular fractionation/immunofluorescence, 53BP1 foci assay |
Science signaling |
High |
25872870
|
| 2015 |
OTUB1 inhibits ubiquitination and proteasomal degradation of FOXM1 through its catalytic (C91-dependent) deubiquitinase activity; the C91S catalytic mutant fails to stabilise FOXM1, increase its half-life, or enhance proliferative and epirubicin-resistance phenotypes. |
Co-immunoprecipitation, siRNA knockdown and overexpression, cycloheximide chase, catalytic mutant (C91S), K48-ubiquitin linkage analysis |
Oncogene |
High |
26148240
|
| 2016 |
OTUB1 inhibits RAS mono- and di-ubiquitination independently of its catalytic activity, resulting in sequestration of RAS on the plasma membrane and enhanced RAS activation and ERK1/2 signalling, thereby promoting tumorigenesis in wild-type RAS cells. |
In vitro ubiquitination assays, catalytic mutant analysis, confocal microscopy for RAS membrane localisation, RAS-GTP pull-down, tumour xenograft assays |
EMBO molecular medicine |
High |
26881969
|
| 2016 |
FIH (factor inhibiting HIF) hydroxylates OTUB1 at asparagine 22; mutation of N22 profoundly alters OTUB1 protein interaction network and impairs cellular metabolic processes, identifying OTUB1 as a non-HIF substrate whose activity is regulated by oxygen-dependent hydroxylation. |
In vitro hydroxylation assays, N22A mutant co-immunoprecipitation proteomics, cellular metabolic assays (oxygen consumption, glycolysis) |
PLoS biology |
Medium |
26752685
|
| 2018 |
OTUB1 directly interacts with DEPTOR via its N-terminal domain, deubiquitinates DEPTOR in a Cys91-independent but Asp88-dependent (non-canonical) manner, stabilises DEPTOR, and thereby suppresses amino-acid-induced mTORC1 activation, cellular autophagy, and cell proliferation/size. |
In vitro deubiquitination assay, co-immunoprecipitation, catalytic-dead and D88A mutant analysis, mTORC1 activity assays (S6K phosphorylation), autophagy assays |
The Journal of biological chemistry |
High |
29382726
|
| 2018 |
OTUB1 stabilises Snail by preventing its ubiquitination and proteasomal degradation, facilitating epithelial-mesenchymal transition and metastasis of esophageal squamous cell carcinoma cells. |
Co-immunoprecipitation, siRNA/overexpression, ubiquitination assays, invasion/migration assays |
Oncogene |
Medium |
29559747
|
| 2018 |
OTUB1 non-canonically stabilises the E2 enzyme UBE2E1 by suppressing its autoubiquitination in vitro and in cells, preventing proteasomal degradation of UBE2E1; this function is independent of OTUB1 catalytic activity but requires its ability to bind UBE2E1. Otub1 knockout mice exhibit late-stage embryonic lethality. |
In vitro autoubiquitination assay, OTUB1 KO cell lines (mouse and human), cycloheximide chase, catalytic mutant and binding-defective mutant analysis, mouse knockout |
The Journal of biological chemistry |
High |
30282802
|
| 2019 |
OTUB1 directly interacts with SLC7A11 (xCT), a key component of the cystine-glutamate antiporter, and stabilises SLC7A11 protein. CD44 overexpression enhances the OTUB1–SLC7A11 interaction, while CD44 depletion partially abrogates it. OTUB1 knockdown destabilises SLC7A11 and promotes ferroptosis in cancer xenografts. |
Biochemical purification/mass spectrometry to identify OTUB1 as SLC7A11-binding partner, Co-IP, siRNA knockdown, xenograft tumour growth assays, ferroptosis markers |
Cancer research |
High |
30709928
|
| 2019 |
FIH forms an oxygen-sensitive, likely covalent (co-translational amide) bond with OTUB1 within cells, generating a heterotrimeric complex of two FIH and one OTUB1; this complexation regulates OTUB1 deubiquitinase activity in an oxygen-dependent manner, providing a mechanism for hypoxia adaptation. |
Biochemical co-precipitation, mass spectrometry analysis of bond, co-expression in mammalian and bacterial cells, DUB activity assays, oxygen-dependency experiments |
Redox biology |
Medium |
31299612
|
| 2019 |
IL-15 induces membrane recruitment of Otub1, which then non-canonically inhibits ubiquitin-dependent AKT activation, setting a threshold for CD8+ T cell and NK cell activation; Otub1 deficiency causes AKT hyperactivation, enhanced T cell metabolic reprogramming, and augmented anti-cancer immunity. |
Conditional Otub1 KO mice, IL-15 stimulation assays, membrane fractionation, ubiquitination assays of AKT, T cell and NK cell functional assays, tumour challenge models |
Nature immunology |
High |
31182807
|
| 2019 |
Otub1 stabilises p100 (NF-κB precursor) by preventing its ubiquitination and degradation; Otub1 deficiency causes both increased signal-induced p100 processing (non-canonical NF-κB) and steady-state p100 degradation (leading to aberrant canonical NF-κB activation), resulting in B-cell hyperplasia and lupus-like autoimmunity. |
B cell-conditional Otub1 KO mice, ubiquitination assays, NF-κB pathway activation readouts, immunophenotyping, autoimmunity assessment |
Cell research |
High |
31086255
|
| 2019 |
The ubiquitin-like modifier FAT10 non-covalently interacts with OTUB1 and stimulates its K48-linked DUB activity; FAT10 also strengthens OTUB1's non-catalytic suppression of K63 polyubiquitylation on TRAF3 and increases OTUB1 interaction with UBCH5B, while covalent FAT10ylation leads to OTUB1 proteasomal degradation. |
In vitro DUB activity assays, Co-IP, ubiquitination assays of TRAF3, FAT10 covalent vs. non-covalent interaction analysis |
The Journal of biological chemistry |
Medium |
30718280
|
| 2020 |
OTUB1 removes K48-linked ubiquitin chains from PD-L1 via its catalytic deubiquitinase activity, blocking ERAD-dependent PD-L1 degradation, stabilising PD-L1 at the tumour cell surface, and suppressing CD8+ T cell-mediated cytotoxicity. |
Co-immunoprecipitation, K48-ubiquitin chain-specific deubiquitination assays, OTUB1 KO/knockdown, PD-1 binding assay, PBMC cytotoxicity assay, in vivo tumour model with CD8+ T cell infiltration |
Cell death and differentiation |
High |
33328570
|
| 2020 |
OTUB1 activates RIG-I antiviral signalling via a dual mechanism: hydrolysis of K48-linked polyubiquitin and formation of an E2-repressive complex with UBCH5c. Upon IAV infection, OTUB1 relocalises from the nucleus to mitochondrial membranes together with RIG-I. Influenza A NS1 protein triggers proteasomal degradation of OTUB1 to antagonise this signalling. |
Cell-free reconstitution system with [35S]IRF3, purified RIG-I, mitochondrial membranes, and OTUB1 variants; immunofluorescence for relocalization; OTUB1 CRISPR/knockdown with IFN readouts; NS1 degradation assay |
Cell reports |
High |
32023470
|
| 2020 |
OTUB1 promotes NF-κB activity in dendritic cells through K48-linked deubiquitination and stabilisation of the E2 enzyme UBC13, which in turn increases K63-linked ubiquitination of IRAK1 and TRAF6, augmenting cytokine (IL-6, IL-12, TNF) production upon TLR stimulation. |
DC-specific Otub1 KO mice, ubiquitination assays for UBC13/IRAK1/TRAF6, cytokine measurement, T. gondii infection model |
Cellular & molecular immunology |
High |
32024978
|
| 2020 |
Otub1 directly interacts with c-Maf and abrogates K48-linked polyubiquitination of c-Maf, preventing its degradation and enhancing its transcriptional activity; this deubiquitination depends on Otub1's Lys71 and N terminus but is independent of UBE2O. |
Mass spectrometry identification of Otub1-c-Maf interaction, Co-IP, K48-ubiquitination assays, deletion/point mutant analysis, myeloma cell survival assays |
Blood |
Medium |
32842143
|
| 2021 |
OTUB1 inhibits MSH2 ubiquitination by blocking E2 ubiquitin transfer activity (non-canonical mechanism), maintaining MSH2 protein stability; OTUB1 depletion promotes MSH2 ubiquitination, increases mutation frequency, and causes resistance to genotoxic agents. |
Functional ubiquitination and deubiquitination assays, OTUB1 knockdown, mutation frequency assays, drug sensitivity assays |
The Journal of biological chemistry |
Medium |
33640455
|
| 2021 |
OTUB1 stabilises SOCS1 via K48-linked deubiquitination, thereby inhibiting IFN-γ-induced JAK2/STAT1 signalling hyperactivation in astrocytes. Astrocyte-specific Otub1 KO mice develop more severe EAE due to astrocyte hyperactivation. |
Astrocyte-specific conditional Otub1 KO mice, K48-ubiquitination assays for SOCS1, JAK/STAT signalling readouts, EAE model |
The EMBO journal |
High |
30944096
|
| 2021 |
OTUB1 prevents hepatocyte necroptosis by stabilising c-IAP1 through K48-deubiquitination, thereby maintaining K63-linked ubiquitination of RIPK1 and preventing RIPK1/RIPK3 necrosome formation and MLKL phosphorylation. OTUB1 deletion in liver parenchymal cells causes lethal necroptosis upon bacterial infection or TNF challenge. |
Hepatocyte-specific Otub1 KO mice (OTUB1LPC-KO), human HepG2 OTUB1-KO cells, K48-ubiquitination assay for c-IAP1, RIPK1 K63-ubiquitination, RIPK3/MLKL phosphorylation, necrostatin-1s rescue, MLKL KO rescue |
Cell death and differentiation |
High |
33712742
|
| 2021 |
OTUB1 directly deubiquitinates YAP protein via its OTU domain at multiple lysine sites (K90, K280, K343, K494, K497), stabilising YAP and promoting Hippo pathway suppression in gastric cancer. |
DUB siRNA library screen, Co-IP, in vitro and in vivo deubiquitination assays, site-directed mutagenesis of YAP lysines |
Oncogene |
Medium |
36271031
|
| 2021 |
OTUB1 deubiquitinates and stabilises MYC at the K323 site, preventing its proteasomal degradation; stabilised MYC promotes HK2 expression and aerobic glycolysis in breast cancer. OTUB1-mediated MYC stability is confirmed in OTUB1-knockout mice. |
Co-IP, in vitro deubiquitination assay, site-directed mutagenesis (K323), OTUB1-KO mice, glycolysis assays, in vivo tumorigenesis |
Cell death and differentiation |
High |
35296795
|
| 2022 |
CST1 recruits OTUB1 to GPX4, relieving GPX4 ubiquitination and improving its protein stability; this reduces intracellular ROS and inhibits ferroptosis in gastric cancer cells. The CST1–OTUB1–GPX4 interaction was confirmed by Co-IP combined with mass spectrometry. |
Co-immunoprecipitation combined with mass spectrometry, ubiquitination assay, siRNA knockdown, ROS assays, in vivo metastasis models |
Oncogene |
Medium |
36369321
|
| 2022 |
OTUB1 stabilises HIF-1α under hypoxia via non-canonical inhibition of K48-linked polyubiquitination (independent of PHDs/VHL/FIH); OTUB1 depletion reduces endogenous HIF-1α protein and suppresses hypoxia-induced glycolytic reprogramming. |
Co-IP, K48-ubiquitination assay, OTUB1 knockdown under hypoxia, HIF-1α protein stability assays, glycolysis metabolic assays |
Cell death & disease |
Medium |
35732631
|
| 2022 |
OTUB1 non-canonically stabilises Raptor (mTORC1 component) by preventing its ubiquitination; phosphorylation of OTUB1 at Tyr26 by Src and SRMS kinases is required for the OTUB1–Raptor interaction, and dephosphorylation of OTUB1 at Y26 destabilises Raptor and sensitises cancer cells to anti-cancer drugs via mitochondrial ROS-mediated dysfunction. |
Biochemical interaction assays, Co-IP with Y26 mutant, in vitro kinase assays (Src/SRMS), ubiquitination assays of Raptor, drug sensitivity assays, mitochondrial ROS measurement |
Cell death and differentiation |
Medium |
35927303
|
| 2022 |
Endogenous H2S (produced by CTH) persulfidates OTUB1 at cysteine 91, promoting OTUB1 interaction with the E2 UBCH5A and thereby decreasing ubiquitination and proteasomal degradation of SLC7A11/xCT, increasing cellular glutathione; GLRX reverses this by deglutathionylation (at C23 or C204) of OTUB1. |
S-glutathionylation/persulfidation site-mapping, Co-IP of OTUB1-UBCH5A, ubiquitination and stability assays of SLC7A11, GLRX knockout/overexpression, GSH measurement |
Science advances |
Medium |
37703360
|
| 2023 |
SET7 lysine monomethylase directly interacts with OTUB1 and catalyses its methylation at lysine 122; this modification does not affect OTUB1's DUB catalytic activity but impairs its non-canonical ability to bind UBC13, thereby relieving OTUB1's suppressive role on ferroptosis. |
In vitro methylation assay, site-directed mutagenesis (K122), Co-IP of OTUB1–UBC13, cell viability and intracellular ROS assays |
The Journal of biological chemistry |
Medium |
36822329
|
| 2023 |
OTUB1 non-canonically stabilises TGFBI by deubiquitinating it at K22 and K25 residues in a manner independent of OTUB1 catalytic activity; OTUB1-mediated TGFBI stabilisation promotes glycolysis and angiogenesis in infantile hemangioma. |
Mass spectrometry for substrate identification, Co-IP, ubiquitination assay with site-specific K22/K25 mutagenesis, catalytic mutant analysis, extracellular acidification rate assays, in vivo IH model |
Arteriosclerosis, thrombosis, and vascular biology |
Medium |
36994729
|
| 2024 |
OTUB1 deubiquitinates and stabilises CHK1, enhancing DNA damage repair capacity and conferring radioresistance in lung cancer; OTUB1 depletion impairs DNA damage repair and overcomes radioresistance. |
Co-immunoprecipitation, Western blotting of CHK1 ubiquitination, OTUB1 knockdown with comet assay and immunofluorescence for DNA damage, RNA sequencing, in vivo xenograft with radiotherapy |
International journal of radiation oncology, biology, physics |
Medium |
38266782
|
| 2024 |
OTUB1 non-canonically stabilises RACK1 via inhibition of its K48-linked ubiquitination (independent of catalytic activity), activating PI3K/AKT and FAK/ERK signalling in hepatocellular carcinoma; OTUB1 transcription is driven by the transcription factor MAZ at the OTUB1 promoter. |
Immunoprecipitation-tandem MS for RACK1 identification, Co-IP, K48-ubiquitination assays, catalytic-independent mechanism validation, ChIP-qPCR and dual-luciferase for MAZ-OTUB1 promoter regulation, in vivo xenograft |
Cellular oncology |
Medium |
38315284
|
| 2024 |
OTUB1 non-canonically stabilises YTHDF2 by blocking ubiquitin transfer to it independent of deubiquitinase activity; stabilised YTHDF2 binds and promotes m6A-dependent degradation of PRSS8 mRNA, and PRSS8 loss decreases nuclear β-catenin via E-cadherin, promoting prostate cancer proliferation. |
In vitro and in vivo ubiquitination assays, Co-IP, m6A-seq and transcriptomic analysis, PRSS8 mRNA stability assays, mouse xenograft model |
The Journal of biological chemistry |
Medium |
38462165
|
| 2024 |
Legionella pneumophila effectors SidC/SdcA ubiquitinate OTUB1 at multiple lysine residues, promoting its association with the Legionella-containing vacuole and interaction with DEPTOR, thereby suppressing MTORC1 signalling and promoting host autophagy; SidE family effectors also induce phosphoribosyl-linked ubiquitination of OTUB1 at Ser16/Ser18 to block its DUB activity. |
Biochemical ubiquitination assays with purified effectors, Co-IP of OTUB1-DEPTOR, mTORC1 activity readouts, autophagy assays, BMDM infection model |
Autophagy |
Medium |
38818749
|
| 2014 |
HSCARG promotes OTUB1 recruitment to TRAF3, facilitating TRAF3 deubiquitination by OTUB1 and suppressing RIG-I-like receptor signalling; HSCARG knockout attenuates TRAF3 deubiquitination by OTUB1, and OTUB1 knockdown abolishes the HSCARG-mediated suppression of IFN-β transcription. |
Co-immunoprecipitation, ubiquitination assays of TRAF3, HSCARG KO and OTUB1 KD with IFN-β reporter assays, epistasis experiments |
PLoS pathogens |
Medium |
24763515
|
| 2017 |
Otub1 stabilises MDMX via non-canonical inhibition of MDM2-mediated MDMX ubiquitination (independently of deubiquitinase activity); Otub1-stabilised MDMX localises to mitochondria, enhances p53 phosphorylation at S46, and promotes mitochondria-mediated apoptosis. |
Co-IP, in vitro ubiquitination assay, catalytic mutant analysis, subcellular fractionation, p53-S46 phosphorylation assay, apoptosis assays |
Oncotarget |
Medium |
28035068
|
| 2021 |
OTUB1 suppresses K63-linked ubiquitination of TRAF6 via direct binding, thereby inhibiting the TRAF6-ASK1 signalling axis and protecting against NASH-associated hepatic steatosis, inflammation, and fibrosis. |
Immunoprecipitation-mass spectrometry for TRAF6 identification, Co-IP, K63-ubiquitination assay of TRAF6, hepatocyte-specific Otub1 overexpression mouse model (HFHC diet), Otub1 KO mice |
Hepatology |
Medium |
34591986
|
| 2022 |
ERK/RSK-mediated phosphorylation of YB-1 at Ser102 in hyperglycaemia disrupts its interaction with OTUB1, leading to YB-1 ubiquitination and proteasomal degradation; when the ERK pathway is inhibited, YB-1–OTUB1 interaction is stabilised, preserving YB-1 levels and ameliorating diabetic cardiomyopathy. |
Co-immunoprecipitation, ubiquitination assay of YB-1, phospho-specific YB-1(S102) analysis, ERK inhibitor (U0126) in STZ-diabetic mice, echocardiography |
The Journal of biological chemistry |
Medium |
35490780
|
| 2023 |
OTUB1 non-canonically stabilises CCN6 by inhibiting K48-linked ubiquitination via interaction through its linker domain; OTUB1 deletion reduces CCN6 abundance and increases breast cancer cell migration and proliferation, which is rescued by CCN6 supplementation. |
DUB screening assay, Co-IP, K48-ubiquitination assay, OTUB1 deletion mutants (linker domain), breast cancer cell functional assays, allograft model |
Clinical and translational medicine |
Medium |
37608493
|
| 2025 |
OTUB1 is a novel deubiquitinating enzyme for ERRα; OTUB1 C91 residue is critical for ERRα deubiquitination. The natural product Ailanthone (AIL) inhibits OTUB1 activity by interacting with C91, disrupts the OTUB1–ERRα interaction, and promotes ERRα ubiquitination and proteasomal degradation. |
Competitive activity-based protein profiling (ABPP) for target identification, Co-IP, luciferase reporter assay, C91A mutant analysis, surface plasmon resonance, in vivo TNBC mouse model |
Journal of advanced research |
Medium |
39864589
|