| 2000 |
Ulp1 (yeast ortholog of SENP3) catalyzes two distinct SUMO pathway reactions: (1) processing of full-length SUMO precursor to its mature form, and (2) deconjugation of SUMO from targeted proteins. A covalent thiohemiacetal transition state complex between Ulp1 C-terminal fragment and Smt3 was captured and its crystal structure solved, revealing determinants of SUMO recognition. An N-terminal regulatory element (N-terminal to the proteolytic domain) is required for cell growth in yeast. |
Crystal structure of Ulp1-Smt3 covalent transition-state complex; in vitro proteolytic assays; genetic analysis |
Molecular cell |
High |
10882122
|
| 2000 |
SMT3IP1 (human SENP3) was cloned via yeast two-hybrid with Smt3b as bait. Baculovirus-expressed SMT3IP1 cleaves SUMO-1 and Smt3b from RanGAP1 conjugates in vitro, with slightly stronger activity toward Smt3b (SUMO-2/3) conjugates. The enzyme binds Smt3a and Smt3b more strongly than SUMO-1 in vitro. SMT3IP1 does not cleave Nedd8 or ubiquitin from their conjugates. The N-terminal sequence is responsible for nucleolar localization of the enzyme. |
Yeast two-hybrid cloning; baculovirus expression; in vitro isopeptidase assay on RanGAP1 conjugates; in vitro binding assays; cell fractionation/immunofluorescence for localization |
European journal of biochemistry |
High |
11029585
|
| 2003 |
The N-terminal domain of yeast Ulp1 is necessary and sufficient to concentrate Ulp1 at nuclear envelope (NPC) sites, while the Ulp domain (UD, ~200 residues) alone supports wild-type growth and can cleave SUMO from substrates in vitro. The N-terminal domain restricts Ulp1 activity toward certain sumoylated proteins while enabling cleavage of others, indicating subcellular localization as a physiologically significant constraint on substrate specificity. N-terminally deleted Ulp1 can suppress defects of ulp2Δ cells, unlike full-length Ulp1. |
Domain deletion analysis; in vitro SUMO cleavage assay; in vivo SUMO conjugate profiling; genetic complementation/suppression assays |
The Journal of cell biology |
High |
12654900
|
| 2003 |
Yeast Ulp1 is tethered to nuclear pores via its non-catalytic N-domain, which associates with three karyopherins (Pse1, Kap95, and Kap60) in a complex not dissociated by RanGTP in vitro. The Ulp1 N-domain has two distinct binding sites for Pse1 and Kap95/Kap60, both required for NPC anchoring. The catalytic C-domain of Ulp1 must be excluded from the nucleoplasm for cell viability. |
Co-immunoprecipitation; mass spectrometry interactome; in vitro RanGTP dissociation assay; domain mapping; genetic viability assays |
Nature cell biology |
High |
12471376
|
| 2008 |
SENP3 is a nucleolar SUMO-specific protease associated with nucleophosmin (NPM1). SENP3 catalyzes desumoylation of NPM1-SUMO2 conjugates in vitro and counteracts ARF-induced SUMO2 modification of NPM1 in vivo. Depletion of SENP3 by siRNA inhibits conversion of 32S rRNA to 28S rRNA, phenocopying NPM1 depletion. Constitutive SUMO2 modification of NPM1 interferes with 28S rRNA maturation, defining SENP3 as an essential factor for ribosome biogenesis. |
Co-immunoprecipitation; in vitro desumoylation assay; siRNA knockdown; rRNA processing assay (Northern blot/metabolic labeling) |
EMBO reports |
High |
18259216
|
| 2008 |
SENP3 is a specific interaction partner of Borealin (a chromosomal passenger complex component) and catalyzes removal of SUMO2/3 from Borealin. The SUMO E3 ligase RanBP2 interacts with the CPC, stimulates SUMO modification of Borealin in vitro, and is required for its modification in vivo. This defines a mitotic SUMO2/3 conjugation-deconjugation cycle on Borealin regulated by RanBP2 and SENP3. |
Co-immunoprecipitation; in vitro SUMOylation assay with RanBP2; in vivo SUMOylation analysis; siRNA knockdown; mitotic synchronization |
Molecular biology of the cell |
High |
18946085
|
| 2008 |
B23/nucleophosmin binds SENP3 and SENP5 in Xenopus laevis egg extracts and is essential for stable accumulation of SENP3 and SENP5 in mammalian tissue culture cells. Codepletion of SENP3 and SENP5, or depletion of B23/nucleophosmin, causes accumulation of SUMO proteins within nucleoli and defects in ribosome biogenesis. |
Co-immunoprecipitation in Xenopus extracts; siRNA depletion; SUMO localization by immunofluorescence; ribosome biogenesis assays |
The Journal of cell biology |
High |
19015314
|
| 2008 |
ARF triggers sequential phosphorylation, polyubiquitination, and rapid proteasomal degradation of Senp3 in an NPM-dependent manner. Stabilization of both ARF and Senp3 requires NPM; viable Npm-null cells destabilize both proteins. NPM mutants retaining acidic and oligomerization domains can re-stabilize Senp3. Knockdown of Senp3 mimics the antiproliferative functions of ARF, suggesting SENP3 antagonism mediates p53-independent tumor-suppressive functions of ARF. |
shRNA knockdown; NPM-null MEFs; Western blot for ubiquitination and phosphorylation; NPM domain mutant rescue experiments |
Cell cycle (Georgetown, Tex.) |
Medium |
18948745
|
| 2009 |
SENP3 protein is continuously degraded through the ubiquitin-proteasome pathway under basal conditions; reactive oxygen species (ROS) inhibit this degradation and stabilize SENP3. ROS also causes SENP3 to redistribute from the nucleolus to the nucleoplasm. Stabilized/redistributed SENP3 de-conjugates SUMO2/3 from the HIF-1α co-activator p300 (not HIF-1α itself), which enhances p300 binding to HIF-1α and increases HIF-1 transcriptional activity. |
Cycloheximide chase; proteasome inhibitor treatment; immunofluorescence for subcellular redistribution; siRNA knockdown; co-immunoprecipitation; luciferase reporter; in vivo xenograft |
The EMBO journal |
High |
19680224
|
| 2010 |
SENP3 stability is regulated by interplay between the co-chaperone/E3 ubiquitin ligase CHIP and Hsp90. Under non-stress conditions, CHIP mediates Hsp90-independent ubiquitination and degradation of SENP3. Upon mild oxidative stress, SENP3 undergoes thiol modification, which recruits Hsp90; Hsp90/SENP3 association protects SENP3 from CHIP-mediated ubiquitination, but this protection requires the presence of CHIP. Enhanced SENP3/Hsp90 association is found in cancer cells. |
Co-immunoprecipitation; ubiquitination assay; Hsp90 inhibitor treatment; redox thiol modification assay; Western blot stability assay |
The EMBO journal |
High |
20924358
|
| 2010 |
Low-dose H2O2 induces SENP3 protein accumulation and causes SENP3 to co-localize with PML bodies, resulting in de-conjugation of SUMO2/3 from PML. DeSUMOylation of PML by SENP3 reduces PML body number and is responsible for accelerated cell proliferation under mild oxidative stress; only SUMOylated PML exerts an inhibitory role on proliferation. |
H2O2 treatment; immunofluorescence co-localization; SUMO2/3 de-conjugation assay; siRNA knockdown; SUMOylation-deficient PML mutant rescue |
The Journal of biological chemistry |
Medium |
20181954
|
| 2011 |
SMT3IP1/SENP3 interacts with p53 and Mdm2, and desumoylates both proteins. Overexpression of SMT3IP1 causes Mdm2 accumulation in the nucleolus, increases p53 stability, and suppresses Mdm2-mediated p53 ubiquitination and degradation. SMT3IP1 competes with p53 for binding to the acidic domain of Mdm2. Notably, the desumoylation activity of SMT3IP1 is not required for p53 stabilization. |
Co-immunoprecipitation; overexpression; in vivo ubiquitination assay; nucleolar localization by immunofluorescence; catalytic mutant analysis |
Biochemical and biophysical research communications |
Medium |
21316347
|
| 2012 |
The biphasic redox regulation of HIF-1 transcriptional activity by H2O2 is mediated by differential cysteine modification of SENP3. ROS levels differentially modify cysteines 243 and 532 in SENP3, regulating its interaction with p300 to cause differential p300 SUMOylation and thereby shifting HIF-1 transcriptional activity (enhanced at low ROS, suppressed at high ROS). |
Dose-response H2O2 treatment; luciferase reporter; co-immunoprecipitation; chromatin immunoprecipitation; site-directed mutagenesis of SENP3 cysteines |
Acta pharmacologica Sinica |
Medium |
22684029
|
| 2013 |
SENP3 is degraded during oxygen/glucose deprivation (OGD, an ischemia model) via a pathway involving the UPR kinase PERK and lysosomal enzyme cathepsin B. A key target for SENP3-mediated deSUMOylation is the GTPase Drp1. SENP3 depletion prolongs Drp1 SUMOylation, suppressing Drp1 localization at mitochondria, cytochrome c release, and caspase-mediated cell death. SENP3 recovery upon reoxygenation enables Drp1 deSUMOylation and promotes mitochondrial fragmentation and cell death. |
RNAi knockdown; OGD model; PERK inhibitor; cathepsin B inhibitor; co-immunoprecipitation; mitochondrial fractionation; cytochrome c release assay; caspase activity assay |
The EMBO journal |
High |
23524851
|
| 2014 |
SENP3 controls H3K4 methylation by regulating MLL1/MLL2 histone methyltransferase complexes. SENP3 associates with MLL1/MLL2 complexes and catalyzes deSUMOylation of RbBP5. This is required for activation of HOX genes including DLX3, as SENP3 absence impairs menin and Ash2L association with the DLX3 gene, decreases H3K4 methylation, and reduces RNA polymerase II recruitment. The SENP3-DLX3 pathway governs osteogenic differentiation of human stem cells. |
Co-immunoprecipitation; ChIP; in vivo SUMOylation assay; siRNA knockdown; osteogenic differentiation assay; H3K4 methylation analysis |
Molecular cell |
High |
24930734
|
| 2014 |
mTOR kinase pathway controls the nucleolar targeting of SENP3 by regulating its interaction with NPM1. An N-terminal domain of SENP3 is defined as the critical NPM1 binding region; mTOR-mediated phosphorylation of serine/threonine residues within this region fosters the SENP3-NPM1 interaction. Inhibition of mTOR triggers nucleolar release of SENP3, compromising its activity in rRNA processing. |
mTOR inhibitor (rapamycin/Torin) treatment; domain mapping; co-immunoprecipitation; phosphorylation analysis; rRNA processing assay |
Molecular and cellular biology |
Medium |
25288641
|
| 2014 |
SENP3 promotes epithelial-mesenchymal transition (EMT) in gastric cancer via deSUMOylation of the transcription factor FOXC2. FOXC2 is identified as a SENP3 substrate; deSUMOylation of FOXC2 by SENP3 enhances its transcriptional activity toward N-cadherin. ROS-induced deSUMOylation of FOXC2 is blocked by silencing SENP3. |
Co-immunoprecipitation; in vivo SUMOylation assay; siRNA knockdown and overexpression; EMT marker analysis; migration assay; nude mouse model |
Oncotarget |
Medium |
25216525
|
| 2015 |
SENP3 antagonizes SUMO2/3-targeted ubiquitination of Sp1 mediated by the SUMO-targeted ubiquitin E3 ligase RNF4. DeSUMOylation of Sp1 by SENP3 attenuates Sp1 interaction with RNF4, preventing its proteasomal degradation and increasing Sp1 protein levels. |
Co-immunoprecipitation; ubiquitination assay; siRNA knockdown; Western blot stability assay |
Protein & cell |
Medium |
26511642
|
| 2016 |
SENP3 enhances STAT3 phosphorylation at Y705 by de-conjugating SUMO2/3 from STAT3 at K451. SUMO2/3 modification of STAT3 at K451 facilitates STAT3 binding to the phosphatase TC45 through a SUMO-interacting motif of TC45, thereby dephosphorylating STAT3. SENP3-mediated deSUMOylation of STAT3 prevents TC45 binding and thus enhances STAT3 phosphorylation. |
Co-immunoprecipitation; site-directed mutagenesis (K451); siRNA knockdown; phosphorylation assay; tobacco extract treatment |
Oncogene |
Medium |
27181202
|
| 2017 |
SENP3-mediated deSUMOylation of Drp1 selectively promotes Drp1 binding to the mitochondrial outer membrane adaptor protein Mff. Preventing Drp1 SUMOylation (SUMO acceptor site mutants) enhances Mff binding; increasing SUMOylation by SENP3 knockdown reduces Drp1-Mff binding and stress-induced cytochrome c release. Direct tethering of Drp1 to the mitochondrial outer membrane occludes the effect of SENP3 overexpression. |
Co-immunoprecipitation; SUMO acceptor site mutagenesis; siRNA knockdown; SENP3 overexpression; cytochrome c release assay; mitochondrial tethering construct |
Scientific reports |
Medium |
28262828
|
| 2017 |
FLII (flightless-I homolog, a gelsolin family actin-remodeling protein) associates with SENP3 and the MLL1/2 complex, determines SENP3 recruitment and MLL1/2 complex assembly at the DLX3 gene, and is required for H3K4 methylation, active RNA polymerase II loading, and osteogenic differentiation. |
Co-immunoprecipitation; ChIP; siRNA knockdown; osteogenic differentiation assay |
Epigenetics & chromatin |
Medium |
28344658
|
| 2018 |
SENP3 maintains Treg cell stability and function by controlling SUMOylation and nuclear localization of BACH2. SENP3-mediated deSUMOylation of BACH2 prevents its nuclear export, thereby repressing effector T cell differentiation genes and stabilizing Treg gene signatures. Treg-specific deletion of Senp3 results in T cell activation and autoimmune symptoms. ROS-driven SENP3 accumulation in the tumor microenvironment contributes to Treg-mediated tumor immunosuppression. |
Conditional Senp3 knockout (Treg-specific); co-immunoprecipitation; nuclear/cytoplasmic fractionation; SUMOylation assay; gene expression profiling |
Nature communications |
High |
30089837
|
| 2018 |
SENP3 deficiency in myeloid cells markedly compromises TLR4 inflammatory signaling and JNK phosphorylation in response to LPS. MKK7, which selectively phosphorylates JNK, is a SENP3 substrate; SENP3-mediated deSUMOylation of MKK7 favors its binding to JNK. ROS-dependent SENP3 accumulation and MKK7 deSUMOylation occur rapidly after LPS stimulation. |
Conditional Senp3 KO in myeloid cells; LPS-induced inflammation model; co-immunoprecipitation; JNK phosphorylation assay; septic shock model |
The Journal of biological chemistry |
High |
29352108
|
| 2018 |
Mitotic phosphorylation of SENP3 by Cyclin B-CDK1 suppresses SENP3 deSUMOylation activity toward chromosome-associated proteins including topoisomerase IIα (TopoIIα). Protein phosphatase 1α (PP1α) is the phosphatase that reverses this modification. SENP3 phosphorylation decreases its interaction with TopoIIα. Non-phosphorylatable SENP3 mutant causes mitotic arrest, increased chromosomal instability, and tumorigenesis promotion. |
Kinase identification (CDK1); phosphatase identification (PP1α); co-immunoprecipitation; phospho-mutant analysis; chromosome instability assay; tumorigenesis assay |
Cancer research |
Medium |
29438989
|
| 2019 |
SENP3 deSUMOylates BECN1 (beclin 1) at K380, a SUMO3-conjugation site mediated by PIAS3. BECN1 SUMOylation enhances autophagosome formation by facilitating BECN1 interaction with UVRAG, PIK3C3, and ATG14, promoting PIK3C3 activity. SENP3 deSUMOylates BECN1 to impair BECN1-PIK3C3 complex formation, suppressing PIK3C3 activity and autophagy. Liver-specific Senp3 KO mice show increased autophagy under basal and fasting conditions. |
Liver-specific conditional KO; co-immunoprecipitation; SUMOylation assay; PIK3C3 activity assay; autophagic flux measurement; site-directed mutagenesis (K380) |
Autophagy |
High |
31373534
|
| 2019 |
SENP3 is associated with the SETD7 histone methyltransferase and deSUMOylates SETD7. In muscle cells, SENP3 recruits SETD7 to the sarcomeric MyHC-II gene, promotes SETD7 association with active RNA polymerase II, and precludes the opposing methyltransferase Suv39h1. SENP3 is degraded in cachexia, leading to perturbed MyHC-II expression and disorganized sarcomeres. |
Co-immunoprecipitation; ChIP; in vivo SUMOylation assay; siRNA knockdown; muscle cell contractility assay; cachexia model |
Cell reports |
Medium |
31141694
|
| 2019 |
SUMO1 catalyzes NLRP3 SUMOylation at K204, which facilitates ASC oligomerization, inflammasome activation, and IL-1β secretion. SENP3 is required for deSUMOylation of NLRP3 and, upon deSUMOylation, attenuates ASC recruitment, speck formation, inflammasome activation, and IL-1β cleavage. |
Co-immunoprecipitation; SUMOylation assay; siRNA knockdown; ASC speck formation assay; IL-1β ELISA; site-directed mutagenesis (K204) |
FASEB journal |
Medium |
31914638
|
| 2020 |
p53 suppresses SENP3 phosphorylation in response to DNA damage at G2/M phase. Suppression of SENP3 phosphorylation activates SENP3 deSUMOylation of Cdh1, which promotes Cdh1 dephosphorylation by Cdc14B, activates APC/CCdh1 E3 ligase, and leads to ubiquitination and degradation of Plk1 in the G2 checkpoint pathway. |
Co-immunoprecipitation; SUMOylation assay; phosphorylation analysis; CDK1/CDK2 inhibitors; Cdc14B phosphatase assay; Plk1 ubiquitination assay; G2 arrest assay |
Cell discovery |
Medium |
32351703
|
| 2020 |
SENP3 loss in bone marrow-derived monocytes promotes osteoclast differentiation. Mechanistically, loss of SENP3 increases SUMO3 modification of IRF8 at K310, which upregulates NFATc1 expression and osteoclastogenesis. Myeloid-specific SENP3 KO mice exhibit more severe bone loss after ovariectomy. |
Conditional SENP3 KO (myeloid); SUMOylation assay; site-directed mutagenesis (K310); NFATc1 expression analysis; osteoclast differentiation assay; ovariectomy model |
Cell reports |
High |
32049023
|
| 2021 |
SENP3 senses ROS in dendritic cells (DCs) to facilitate STING-dependent antitumor immunity. DC-derived ROS trigger SENP3 accumulation and the SENP3-IFI204 interaction; SENP3 catalyzes IFI204 deSUMOylation to boost STING signaling activation. DC-specific deletion of Senp3 blunts STING-dependent type-I interferon signaling and dampens antitumor immune responses. |
DC-specific conditional Senp3 KO; co-immunoprecipitation; IFI204 SUMOylation assay; STING signaling assay; IFN-I measurement; tumor growth model |
Molecular cell |
High |
33434504
|
| 2021 |
SENP3 loss in macrophages promotes M2 polarization by causing enhanced Akt1 SUMOylation and hyper-phosphorylation/activation of Akt1. Macrophage-specific deletion of SENP3 in vivo accelerates breast cancer malignancy. |
Conditional SENP3 KO (macrophage-specific); co-immunoprecipitation; Akt1 SUMOylation assay; Akt1 phosphorylation assay; M2 polarization assay; orthotopic tumor model |
Molecular oncology |
Medium |
33932085
|
| 2021 |
SENP3 interacts with β-catenin and inhibits its proteasome-dependent degradation via de-SUMOylation of β-catenin, promoting VSMC proliferation and migration and vascular remodeling. SENP3+/- mice exhibit alleviated vascular remodeling. |
Co-immunoprecipitation; in vivo deSUMOylation assay; siRNA knockdown/overexpression; VSMC proliferation/migration assay; SENP3 heterozygous KO mouse model |
EBioMedicine |
Medium |
34000626
|
| 2021 |
SENP3 promotes Drp1 binding to Bcl-xL at the mitochondrial outer membrane in a manner primed by Mff. DeSUMOylation of Drp1 by SENP3 promotes the Drp1-Bcl-xL interaction in vivo and in vitro. Mff and Bcl-xL can interact directly through their transmembrane domains independent of Drp1. SENP3 loss during OGD correlates with reduced Drp1-Bcl-xL interaction, contributing to cell death after reoxygenation. |
Co-immunoprecipitation; in vitro binding assay; SUMO acceptor site mutants; OGD/reoxygenation model; Bcl-xL transmembrane domain mutant |
Frontiers in cell and developmental biology |
Medium |
34722538
|
| 2022 |
SENP3 is responsible for deSUMOylation of mitochondrial fission protein Fis1 at K149 (a residue critical for Fis1 mitochondrial localization). DFP treatment stabilizes SENP3 via downregulation of the E3 ubiquitin ligase CHIP. SENP3-mediated Fis1 deSUMOylation enhances Fis1 mitochondrial targeting and is required for DFP-induced mitophagy. Fis1 K149R mutation (preventing SUMOylation) enhances mitochondrial localization and restores mitophagy in SENP3-depleted cells. |
siRNA knockdown; co-immunoprecipitation; Fis1 K149R site-directed mutant; mitophagy assay; mitochondrial fractionation; CHIP Western blot |
EMBO reports |
High |
34994490
|
| 2022 |
TIP60 is hyper-SUMOylated under normal conditions; upon irradiation-induced DNA damage, SENP3-mediated deSUMOylation of TIP60 promotes its interaction with DNA-PKcs to form the TIP60-DNA-PKcs complex. This is required for TIP60-mediated acetylation of DNA-PKcs and DNA-PKcs autophosphorylation, enabling NHEJ-mediated DNA damage repair. SENP3 knockdown impairs DNA damage repair. |
Co-immunoprecipitation; TIP60/DNA-PKcs acetylation assay; NHEJ reporter system; comet assay; γH2AX immunofluorescence; clonogenic survival assay |
MedComm |
Medium |
35356800
|
| 2021 |
SENP3 and SENP5 deSUMOylate Aurora A (AurA) at K258, where SUMO2 conjugation in early mitosis promotes AurA kinase activity and facilitates binding with its activator Bora. Knockdown of SENP3 and SENP5 increases AurA SUMOylation, leading to increased kinase activity and abnormalities in spindle assembly and chromosome segregation; these defects are rescued by suppressing AurA kinase activity. |
In vivo and in vitro SUMOylation assay; site-directed mutagenesis (K258); co-immunoprecipitation; kinase activity assay; spindle assembly checkpoint assay; siRNA knockdown |
Journal of cell science |
Medium |
34313310
|
| 2022 |
Mitotic activation of SENP3 (by prevention of inhibitory phosphorylation) in tumor cells increases micronuclei formation, which activates cGAS signaling-dependent innate immune response and increases CD8+ T cell infiltration. p53 responding to DNA damage activates mitotic SENP3 by inhibiting its phosphorylation, further increasing cellular senescence and innate immune response. |
Phospho-mutant SENP3 expression; micronuclei quantification; cGAS-STING pathway assay; immune-competent mouse tumor model; CD8+ T cell flow cytometry |
Cell death & disease |
Medium |
35869062
|
| 2023 |
The enzymatic activity of SENP3 is required for deSUMOylation of rixosome subunits, which is necessary for association of the rixosome with PRC1 and for silencing of Polycomb target genes. Both SENP3 and USP7 enzymatic activities are required for Polycomb- and rixosome-dependent silencing at an ectopic reporter locus. |
Co-immunoprecipitation; SUMOylation assay; siRNA knockdown with catalytic mutant rescue; reporter silencing assay; ChIP |
Cell reports |
Medium |
37014752
|
| 2023 |
The Brucella effectors NyxA and NyxB directly interact with SENP3 via a defined acidic patch (identified by crystal structure of NyxB) and prevent nucleolar localization of SENP3 at late stages of infection. By sequestering SENP3, the effectors promote cytoplasmic accumulation of nucleolar AAA-ATPase NVL and ribosomal protein RPL5. SENP3 normally regulates the subcellular localization of these nucleolar proteins through its SUMO protease activity; the Beclin1 and PIAS3 were also found to be required for the effector-dependent shuttling. |
Crystal structure of NyxB-acidic patch; co-immunoprecipitation; SENP3 localization by immunofluorescence; NVL/RPL5 localization analysis; genetic epistasis with Beclin1 and PIAS3 |
Nature communications |
High |
36609656
|
| 2023 |
SENP3-mediated deSUMOylation of c-Jun activates its transcriptional activity and the MAPK/AP-1 signaling pathway in microglia following cerebral ischemia. Microglia-specific SENP3 knockdown reduces neuroinflammation, infarct volume, and neurological deficits after ischemic stroke. |
Co-immunoprecipitation; deSUMOylation assay; microglia-specific KD; cytokine measurement; infarct volume measurement |
iScience |
Medium |
37332598
|
| 2024 |
SENP3 deSUMOylates RACK1, increasing RACK1 stability and its interaction with PKCβII, thereby promoting eIF4E phosphorylation and translation of oncogenes (Bcl2, Snail, Cyclin D1) in hepatocellular carcinoma. SENP3 also promotes CCL20 translation via the RACK1/eIF4E axis, facilitating tumor-associated macrophage infiltration and immune evasion. |
Co-immunoprecipitation; SUMOylation assay; RACK1 stability assay; eIF4E phosphorylation assay; liver-specific SENP3 KD; chemically induced HCC model |
Cell death and differentiation |
Medium |
39755756
|
| 2024 |
SENP3 promotes hypoxia-induced mitophagy (HIM) through deSUMOylation of FIS1. Under hypoxia, FIS1 SUMO2/3-ylation promotes interaction with Rab GAP protein TBC1D17, which suppresses HIM. SENP3-mediated FIS1 deSUMOylation counteracts TBC1D17-mediated suppression, promoting mitophagy and cell survival under hypoxia. |
Co-immunoprecipitation; FIS1 SUMOylation assay; TBC1D17 interaction assay; mitophagy assay; hypoxia model; siRNA knockdown; glioblastoma patient-derived cultures |
Cell death & disease |
Medium |
39638786
|
| 2025 |
SENP3 deSUMOylates CTH (Cystathionine Gamma-Lyase) at K361, facilitating its proteasome-dependent degradation. SUMO-3 modification of CTH at K361 promotes CTH protein stability. SENP3-mediated CTH degradation reduces H2S production, promoting macrophage ferroptosis and inflammation in abdominal aortic aneurysm. SENP3 expression is negatively regulated by the E3 ubiquitin ligase STUB1/CHIP. |
Co-immunoprecipitation; SUMOylation assay; site-directed mutagenesis (K361); CTH stability assay; myeloid-specific SENP3 KO; AAA mouse models (AngII and CaCl2); ferroptosis assay |
Advanced science |
Medium |
40019399
|