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Data suggest that SENP2 in hepatic stellate cells is involved in regulation of apoptosis in these cells and in development/reversion of liver fibrosis (here, carbon tetrachloride-induced liver fibrosis).
Expression of the SENP2 gene was suppressed by theobromine. In vivo knockdown studies showed that AR1 knockdown in mice attenuated the anti-adipogenic effects of theobromine in younger mice. Theobromine suppresses adipocyte differentiation and induced C/EBPbeta degradation by increasing its sumoylation.
SENP2 regulates Drp1 sumoylation and stability critical for mitochondrial morphogenesis.SENP2 plays role in mitochondria mediated neural degeneration.
This study identified an animal model of SUDEP, which is caused by alteration of a posttranslational protein modification pathway (SUMOylation) on a unique voltage-gated potassium channel (Kv7.2/Kv7.3)
These results reveal the important role of SENP2 in the regulation of myostatin expression and myogenesis.
SENP2 represses glycolysis and shifts glucose metabolic strategy
Data suggest that SENP2 regulates antiviral innate immunity by deSUMOylating IRF3 and conditioning it for ubiquitination and degradation, and provide an example of cross-talk between the ubiquitin and SUMO pathways in innate immunity.
a mechanism underlying the SENP2-mediated regulation of Mdm2 that is critical for genome integrity in p53-dependent stress responses.
SENP2 de-SUMOylates PPARgamma in myotubes, and de-SUMOylation of PPARgamma selectively increases the expression of some PPARgamma target genes.
Senp2 is essential for suppression of polycomb group protein-mediated gene silencing during embryonic development.
These results establish a critical role for SENP2 in the regulation of adipogenesis by desumoylation.
SUMO-1 protease-1 regulates gene transcription through PML.
data reveal a key genetic pathway, SENP2-Mdm2-p53, underlying trophoblast lineage development, suggesting its pivotal role in cell cycle progression of mitosis and endoreduplication.
he nuclear factor (NF)kappaB signaling pathway was also regulated by the overexpression of SENP2. On the whole, the findings of this study indicate tha SENP2 can act as a tumor suppressor in CLL cells, and may thus prove to be a novel target for CLL treatment in clinical practice.
SENP2 is amplified as part of the chromosome 3q amplification in many cancers and Increased SENP2 expression prolongs MDC1 focus retention and increases NHEJ and radioresistance
SENP2 binds to intracellular membranes where it interacts with membrane-associated proteins and has the potential to regulate their sumoylation and membrane-associated functions.
research achievements of SENP2 are reviewed in order to understand its related functions and the underlying molecular mechanisms and provide a clue for future research on SENP2
Quantitative high-throughput screening identifies cytoprotective molecules that enhance SUMO conjugation via the inhibition of SUMO-specific protease (SENP)2.
Data show that Sentrin/SUMO specific protease (SENP2) interacts with N-myc downstream regulated gene 2 (NDRG2) and mediates the de-SUMOylation process of NDRG2.
Data demonstrate that downregulation of SENP2 is correlated with poor prognosis in bladder cancer; SENP2 inhibits TGF-beta signaling and TGF-beta-induced EMT of bladder cancer cell; and that its overexpression contributes to suppress bladder cancer cell invasion and metastasis through deSUMOylation of TGF-betaRI.
The variability of the SENP1 and SENP2 genes may play a role in breast cancer occurrence.
SENP2 inhibits MMP13 expression in BC cells through de-SUMOylation of TBL1/TBLR1, which inhibits nuclear translocation of beta-catenin.
miR-181b targets SENP2 and positively regulated NF-kappaB activity. NF-kappaB activation by DNA damage in GBM cells confers resistance to radiation-induced death.
data identify SENP2 as an important regulator of fatty acid metabolism in skeletal muscle
SENP2 regulates the transcriptional function of MEF2A via direct de-SUMOylation.
p90RSK-mediated SENP2-T368 phosphorylation is a master switch in disturbed-flow-induced signaling.
we show that WWOX required for stabilization of beta-catenin regulated by SENP2 in hepatocellular carcinoma cells
ESR1 repression by SENP2 is independent of its SUMO protease activity.
Many nucleoporins are mislocalized and, in some cases, reduced in level when SENP1 and SENP2 are codepleted.
Chromosome segregation depends on precise spatial and temporal control of sumoylation in mitosis; SENP1 and SENP2 are important mediators of this control.
The SENP1 levels are influenced by the presence of Nup153, whereas SENP2 is not sensitive to changes in Nup153 abundance.
SENP2 inhibited bladder cancer cells migration and invasion by regulating the expression of MMP13.
SENP2 plays an important role in determining the dynamics and functional outcome of MEF2A SUMOylation and transcriptional activation.
SUMO1 (UBL1\; MIM 601912) is a small ubiquitin-like protein that can be covalently conjugated to other proteins. SENP2 is one of a group of enzymes that process newly synthesized SUMO1 into the conjugatable form and catalyze the deconjugation of SUMO1-containing species.
SUMO-1 protease 1
, SUMO-1 protease-1
, SUMO-1/Smt3-specific isopeptidase 2
, SUMO/sentrin specific protease 2
, sentrin-specific protease 2
, sentrin/SUMO-specific protease SENP2
, SMT3-specific isopeptidase 2
, SUMO1/sentrin/SMT3 specific protease 2
, Axin-associating molecule
, SUMO/sentrin specific peptidase 2