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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.

SUMO1/sentrin/SMT3 specific peptidase 3

SENP3, SSP3, SMT3IP1, Smt3-specific isopeptidase, Smt3-specific isopeptidase 1
The reversible posttranslational modification of proteins by the addition of small ubiquitin-like SUMO proteins (see SUMO1; MIM 601912) is required for numerous biologic processes. SUMO-specific proteases, such as SENP3, are responsible for the initial processing of SUMO precursors to generate a C-terminal diglycine motif required for the conjugation reaction. They also have isopeptidase activity for the removal of SUMO from high molecular mass SUMO conjugates (Di Bacco et al., 2006 [PubMed 16738315]).[supplied by OMIM, Jun 2009] (from NCBI)
Top mentioned proteins: Smt3, Ubiquitin, SUMO-2, CAN, V1a
Papers on SENP3
SENP3 regulates the global protein turnover and the Sp1 level via antagonizing SUMO2/3-targeted ubiquitination and degradation.
New
Yi et al., Shanghai, China. In Protein Cell, Jan 2016
The present study investigated the role of SENP3 in the global protein turnover related to SUMO2/3-targeted ubiquitination and focused in particular on the SENP3 regulation of the stability of Sp1.
Evaluation of the activity and substrate specificity of the human SENP family of SUMO proteases.
New
Pinto et al., Porto, Portugal. In Biochim Biophys Acta, Jan 2016
We found that SENP1 is by far the most versatile and active SENP whereas SENP3 stands out as the least active of these enzymes.
Inhibition of SENP3 by lentivirus induces suppression of apoptosis in experimental subarachnoid hemorrhage in rats.
New
Hang et al., Nanjing, China. In Brain Res, Nov 2015
SUMO-specific proteases 3 (SENP3), a member of the small ubiquitin-like modifier specific protease family, was identified as an isopeptidase that deconjugates SUMOylation (The covalent modification by SUMO) of modified protein substrates.
Psoriatic T cells reduce epidermal turnover time and affect cell proliferation contributed from differential gene expression.
New
Zhang et al., Taiyuan, China. In J Dermatol, Sep 2015
Psoriatic T cells exhibited the ability to decrease epidermal turnover time and affect keratinocyte proliferation because of the differential expression of PPIL1, HSPH1, SENP3, NUP54, FABP5, PLEKHG3, SLC9A9 and CHCHD4.
SUMOylation and Ubiquitylation Circuitry Controls Pregnane X Receptor Biology in Hepatocytes.
New
Staudinger et al., United States. In Drug Metab Dispos, Sep 2015
The SUMO modification of PXR is effectively antagonized by the SUMO protease sentrin protease (SENP) 2, whereas SENP3 and SENP6 proteases are highly active in the removal of SUMO2/3 chains.
Expression and Cell Distribution of SENP3 in Brain Tissue After Traumatic Brain Injury in Mice: A Pilot Study.
New
Hang et al., Nanjing, China. In Cell Mol Neurobiol, Jul 2015
SUMO-specific proteases 3 (SENP3) is a member of the small ubiquitin-like modifier-specific protease family and deconjugates SUMO2/3 from protein substrates.
Expression and cell distribution of SENP3 in the cerebral cortex after experimental subarachnoid hemorrhage in rats: a pilot study.
New
Hang et al., Nanjing, China. In Cell Mol Neurobiol, Apr 2015
Small ubiquitin-like modifier (SUMO)-specific proteases 3 (SENP3), a member of the SUMO-specific protease family, was identified as an isopeptidase that deconjugates SUMOylation (The covalent modification by SUMO) of modified protein substrates.
mTOR signaling regulates nucleolar targeting of the SUMO-specific isopeptidase SENP3.
Muller et al., Frankfurt am Main, Germany. In Mol Cell Biol, 2014
One critical factor of 28S rRNA maturation is the SUMO-isopeptidase SENP3.
The SUMO Protease SENP3 Orchestrates G2-M Transition and Spindle Assembly in Mouse Oocytes.
Huo et al., Wuhan, China. In Sci Rep, 2014
SENP3 an important deSUMOylation protease has been intensively studied in ribosome biogenesis and oxidative stress.
Global implementation of two shared socioeconomic pathways for future sanitation and wastewater flows.
Lucas et al., Utrecht, Netherlands. In Water Sci Technol, 2014
SSP1 is a scenario that includes improvement of wastewater treatment and SSP3 does not include such improvement, with fewer investments and a higher population growth.
De-SUMOylation of FOXC2 by SENP3 promotes the epithelial-mesenchymal transition in gastric cancer cells.
Yi et al., Shanghai, China. In Oncotarget, 2014
Our previous study shows that SENP3, a redox-sensitive SUMO2/3-specific protease, accumulates in a variety of cancers, but whether SENP3 and SUMOylation involve in the regulation of EMT is unclear.
The biphasic redox sensing of SENP3 accounts for the HIF-1 transcriptional activity shift by oxidative stress.
GeneRIF
Yi et al., Shanghai, China. In Acta Pharmacol Sin, 2012
The shift of HIF-1 transactivation by reactive oxidative species is correlated with and dependent on the biphasic redox sensing of SENP3 that leads to the differential SENP3/p300 interaction and the consequent fluctuation in the p300 SUMOylation status.
Redox sensing by proteins: oxidative modifications on cysteines and the consequent events.
Review
Yi et al., Shanghai, China. In Antioxid Redox Signal, 2012
Among dozens of redox sensing proteins listed in this article, SENP3 and caspase-9, which have been investigated in our work, are given particular attention.
SUMO routes ribosome maturation.
Review
Muller et al., Martinsried, Germany. In Nucleus, 2011
In particular, removal of SUMO from trans-acting factors by the SUMO-specific isopeptidase SENP3 is instrumental in the 60S maturation pathway in mammals.
The nucleolar SUMO-specific protease SMT3IP1/SENP3 attenuates Mdm2-mediated p53 ubiquitination and degradation.
GeneRIF
Yamada et al., Tsu, Japan. In Biochem Biophys Res Commun, 2011
These results suggest that SMT3IP1 is a new regulator of the p53-Mdm2 pathway.
Coronin 2A mediates actin-dependent de-repression of inflammatory response genes.
Impact
Glass et al., San Diego, United States. In Nature, 2011
Intriguingly, the LXR transrepression pathway can itself be inactivated by inflammatory signals that induce calcium/calmodulin-dependent protein kinase IIγ (CaMKIIγ)-dependent phosphorylation of LXRs, leading to their deSUMOylation by the SUMO protease SENP3 and release from CORO2A.
Redox regulation of the stability of the SUMO protease SENP3 via interactions with CHIP and Hsp90.
GeneRIF
Yi et al., Shanghai, China. In Embo J, 2010
Hsp90/SENP3 association protects SENP3 from CHIP-mediated ubiquitination and subsequent degradation, but this effect of Hsp90 requires the presence of CHIP.
SENP1 participates in the dynamic regulation of Elk-1 SUMOylation.
GeneRIF
Sharrocks et al., Manchester, United Kingdom. In Biochem J, 2010
Results demonstrate that SENP1 is the most efficient SUMO protease acting on Elk-1, and that SENP3 has little effect on Elk-1. SENP2 has an intermediate effect, but its ability to activate Elk-1 is independent from its SUMO-deconjugating activity.
SENP3-mediated de-conjugation of SUMO2/3 from promyelocytic leukemia is correlated with accelerated cell proliferation under mild oxidative stress.
GeneRIF
Yi et al., Shanghai, China. In J Biol Chem, 2010
SENP3-mediated de-conjugation of SUMO2/3 from promyelocytic leukemia is correlated with accelerated cell proliferation under mild oxidative stress.
FRET-based in vitro assays for the analysis of SUMO protease activities.
Review
Hay et al., Dundee, United Kingdom. In Methods Mol Biol, 2008
In humans cells three SUMO paralogues (SUMO-1, SUMO-2 and SUMO-3) and six SUMO specific proteases (SENP1-SENP3 and SENP5-SENP7) are expressed.
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