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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

SUMO1/sentrin/SMT3 specific peptidase 2

SENP2, SuPr-1, sentrin-specific protease
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.[supplied by OMIM, Apr 2004] (from NCBI)
Top mentioned proteins: Smt3, Ubiquitin, DAPI, SENP1, CAN
Papers on SENP2
The Key Regulator for Language and Speech Development, FOXP2, is a Novel Substrate for SUMOylation.
Yang et al., Birmingham, United States. In J Cell Biochem, Feb 2016
Furthermore, SUMOylation of FOXP2 was significantly decreased by SENP2 (a specific SUMOylation protease).
Disturbed flow-induced endothelial pro-atherogenic signaling via regulating post-translational modifications and epigenetic events.
Abe et al., Houston, United States. In Antioxid Redox Signal, Jan 2016
In addition, PKCζ activation plays a role in regulating SUMOylation-related enzymes of PIAS4, p90RSK activation plays a role in regulating SUMOylation-related enzymes of SENP2, and DNA methyltransferase, SUMOylation may play a role in d-flow signaling.
SENP1 regulates hepatocyte growth factor-induced migration and epithelial-mesenchymal transition of hepatocellular carcinoma.
Wang et al., Shenyang, China. In Tumour Biol, Jan 2016
In this study, we demonstrated that HCC cells express a high level of SUMO/sentrin-specific protease 1 (Senp1) which is induced by HGF/c-Met signals.
Biochemical Characterization and Substrate Specificity of Autophagin-2 from the Parasite Trypanosoma cruzi.
Turk et al., Ljubljana, Slovenia. In J Biol Chem, Dec 2015
Althoughthese substrates were cleaved by cathepsins, making them unsuitable for analysis of complex cellular systems, they were recognized exclusively by TcAtg4.2, but not by HsAtg4B nor by the structurally related human proteases SENP1, SENP2, and UCH-L3.
A novel robust quantitative Förster resonance energy transfer assay for protease SENP2 kinetics determination against its all natural substrates.
Liao et al., Riverside, United States. In Mol Biosyst, Dec 2015
In this paper we report a novel quantitative FRET-based protease assay for SENP2 endopeptidase activity that accounts for the self-fluorescent emissions of the donor (CyPet) and the acceptor (YPet).
DeSUMOylation: An Important Therapeutic Target and Protein Regulatory Event.
Huo et al., Wuhan, China. In Dna Cell Biol, Nov 2015
The critical step in reversing the SUMOylation pathway is its ability to be dynamically deSUMOylated by SUMO/sentrin-specific protease (SENP).
SUMO-Specific Protease 2 (SENP2) Is an Important Regulator of Fatty Acid Metabolism in Skeletal Muscle.
Park et al., Seoul, South Korea. In Diabetes, Jul 2015
Here, we investigated the role of SENP2 in fatty acid metabolism in C2C12 myotubes and in vivo.
Functional Proteomics Study Reveals SUMOylation of TFII-I is Involved in Liver Cancer Cell Proliferation.
He et al., Shanghai, China. In J Proteome Res, Jul 2015
PIAS4 was an E3 ligase for TFII-I SUMOylation, and SENP2 was responsible for deSUMOylating TFII-I in HepG2 cells.
SUMOylation regulates ciliary localization of olfactory signaling proteins.
Martens et al., Gainesville, United States. In J Cell Sci, Jun 2015
Functionally, overexpression of the SUMO protease SENP2 prevented ciliary localization of AC3, without affecting ciliation or cilia maintenance.
MEL-18 loss mediates estrogen receptor-α downregulation and hormone independence.
Kong et al., In J Clin Invest, May 2015
MEL-18 facilitated the deSUMOylation process by inhibiting BMI-1/RING1B-mediated ubiquitin-proteasomal degradation of SUMO1/sentrin-specific protease 1 (SENP1).
Disturbed flow-activated p90RSK kinase accelerates atherosclerosis by inhibiting SENP2 function.
Abe et al., In J Clin Invest, Apr 2015
We have previously shown that d-flow increases SUMOylation of p53 and ERK5 through downregulation of sentrin/SUMO-specific protease 2 (SENP2) function; however, it is not known how SENP2 itself is regulated by d-flow.
Sumoylated HSP90 is a dominantly inherited plasma cell dyscrasias risk factor.
Kubuschok et al., In J Clin Invest, 2015
We determined that the HSP90-SUMO1 carrier state is autosomal-dominantly inherited and caused by the inability of SUMO peptidase sentrin/SUMO-specific protease 2 (SENP2) to desumoylate HSP90-SUMO1.
DNA damage-induced NF-κB activation in human glioblastoma cells promotes miR-181b expression and cell proliferation.
Xu et al., Dalian, China. In Cell Physiol Biochem, 2014
Knockdown SENP2 expression enhanced NF-κB essential modulator (NEMO) SUMOylation and NF-κB activity following IR exposure.
SENP2 regulates MMP13 expression in a bladder cancer cell line through SUMOylation of TBL1/TBLR1.
Qiu et al., Shanghai, China. In Sci Rep, 2014
Recently, we reported that small ubiquitin related modifier (SUMO)-specific protease 2 (SENP2) was downregulated in BC specimen.
Linking the SUMO protease SENP5 to neutrophil differentiation of AML cells.
Tschan et al., Bern, Switzerland. In Leuk Res Rep, 2014
In an mRNA profiling screen performed to unveil novel mechanisms of leukemogenesis, we found that the sentrin-specific protease 5 (SENP5) was significantly repressed in clinical acute myeloid leukemia when compared to healthy neutrophil samples.
Enhanced desumoylation in murine hearts by overexpressed SENP2 leads to congenital heart defects and cardiac dysfunction.
Wang et al., Houston, United States. In J Mol Cell Cardiol, 2012
cardiac overexpression of SENP2 in the mice with Nkx2.5 haploinsufficiency promoted embryonic lethality and severity of congenital heart diseases (CHDs).
The SUMO-specific isopeptidase SENP2 associates dynamically with nuclear pore complexes through interactions with karyopherins and the Nup107-160 nucleoporin subcomplex.
Matunis et al., Baltimore, United States. In Mol Biol Cell, 2011
The SUMO-specific isopeptidase SENP2 associates dynamically with nuclear pore complexes through interactions with karyopherins and the Nup107-160 nucleoporin subcomplex.
SENP2 negatively regulates cellular antiviral response by deSUMOylating IRF3 and conditioning it for ubiquitination and degradation.
Shu et al., Wuhan, China. In J Mol Cell Biol, 2011
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.
NF-κB induction of the SUMO protease SENP2: A negative feedback loop to attenuate cell survival response to genotoxic stress.
Miyamoto et al., Madison, United States. In Mol Cell, 2011
SENP2 null cells display biphasic NEMO SUMOylation and activation of IKK and NF-kappaB
SUMO-specific protease 2 in Mdm2-mediated regulation of p53.
Hsu et al., Rochester, United States. In Cell Death Differ, 2011
a mechanism underlying the SENP2-mediated regulation of Mdm2 that is critical for genome integrity in p53-dependent stress responses.
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