Ask about this productRelated genes to: SENP3 antibody
- Gene:
- SENP3 NIH gene
- Name:
- SUMO specific peptidase 3
- Previous symbol:
- -
- Synonyms:
- DKFZP586K0919, SSP3, DKFZp762A152, SMT3IP1, Ulp1
- Chromosome:
- 17p13
- Locus Type:
- gene with protein product
- Date approved:
- 2004-03-11
- Date modifiied:
- 2018-02-23
Related products to: SENP3 antibody
Related articles to: SENP3 antibody
- Spinal cord injury (SCI) leads to persistent neurological deficits in patients, and effective clinical interventions remain limited. This study aims to elucidate the role and regulatory mechanisms of H6PD in SCI progression, thereby providing insights for developing novel therapeutic strategies. Functional recovery after SCI was assessed using BBB scores, inclined plane tests, and rotarod tests. Spinal cord pathology was evaluated through HE and Nissl staining. The ECAR and OCR were measured using the Seahorse XF96 analyzer. Intracellular ROS levels were detected with DCFH-DA fluorescent probes. Lactate levels, NADPH/NADP ratios, and the levels of MDA, GSH, and SOD were determined using commercial kits. Apoptosis was analyzed by flow cytometry. Protein interactions and SUMOylation levels were examined by Co-IP. H6PD was compensatorily upregulated in SCI rats. H6PD knockdown aggravated neurological deficits and tissue damage. In HO-induced primary neurons, H6PD knockdown enhanced glycolysis, oxidative damage, and apoptosis. Mechanistically, SENP3 interacted with H6PD and promoted its deSUMOylation to inhibit its protein stability. Furthermore, SENP3 exacerbated HO-induced neuronal oxidative damage, apoptosis, and glycolytic abnormalities by downregulating H6PD and disrupting the SIRT1/HIF-1α pathway. SENP3 aggravated neuronal injury and glycolytic dysfunction in SCI by promoting H6PD deSUMOylation and impairing the SIRT1/HIF-1α pathway. - Source: PubMed
Jiang NiTang YunGui Yu-ChangYao Jing-ZhiFang Cui-NiSong TaoXu Jian-Wen - [This corrects the article DOI: 10.3389/fonc.2022.972969.]. - Source: PubMed
Publication date: 2026/05/12
Zhu YouzhiZhang JiashengYu LiangfeiXu SunwangChen LingWu KunlinKong LingjunLin WeiXue JiajieWang QingshuiLin YaoChen Xiangjin - Intestinal ischemia/reperfusion (I/R) causes epithelial oxidative injury, barrier dysfunction, and apoptotic loss, yet its post-translational basis remains poorly understood. SUMOylation is a reversible post-translational process that modulates protein stability and intracellular signaling under stress. However, the role and mechanism of SENP3, a redox-sensitive deSUMOylase, in intestinal I/R remain unclear. In this study, we examined the contribution of SENP3 to intestinal I/R and its mechanism. SENP3 abundance increased substantially in intestinal tissue of mice subjected to I/R and epithelial cells subjected to hypoxia/reoxygenation (H/R). Moreover, blockade of hydrogen peroxide signaling reduced the H/R-induced increase in SENP3 protein without materially altering its mRNA level, suggesting peroxide-associated redox-dependent regulation primarily at the post-transcriptional level. Functionally, SENP3 knockdown alleviated mucosal injury, reduced epithelial apoptosis, and mitigated remote organ damage. Transcriptomic profiling revealed enrichment of the PI3K-Akt pathway following SENP3 knockdown. Additionally, PDPK1, a critical regulator of this pathway, was identified as a SENP3-interacting protein by immunoprecipitation-mass spectrometry and validated by co-immunoprecipitation. SENP3 promoted PDPK1 deSUMOylation in a catalytically dependent manner, leading to increased K48-linked ubiquitination and proteasomal degradation. Site-directed mutagenesis identified Lys296 as a major SUMOylation site on PDPK1. Consequently, SENP3-mediated PDPK1 destabilization suppressed PI3K-Akt signaling, whereas SENP3 inhibition preserved PDPK1 levels and downstream survival signaling. These findings support a SUMO-ubiquitin switch mechanism whereby SENP3-mediated deSUMOylation facilitates ubiquitin-dependent degradation of PDPK1. Overall, our findings define a SENP3-PDPK1-PI3K-Akt regulatory axis linking oxidative stress to epithelial apoptosis during intestinal I/R and support SENP3 as a candidate target for maintaining barrier integrity and reducing reperfusion-related injury. - Source: PubMed
Publication date: 2026/05/14
Liu RenwuLuan QinrongTian Xiaofeng - Protein inhibitor of activated STAT 1 (PIAS1) functions as a SUMO E3 ligase, regulating cardiovascular diseases by promoting the SUMOylation of target proteins; however, its role in abdominal aortic aneurysm (AAA) remains unclear. Currently, molecular targeted therapies for AAA are still very limited. This study aimed to clarify whether PIAS1 regulates the stability of the PPARγ protein through SUMOylation to elucidate its molecular mechanisms in AAA formation and to evaluate its potential as a novel therapeutic target. - Source: PubMed
Publication date: 2026/05/07
Wang HaohuaDai RuiningWang JinWu KunYang BinFeng YaoyuZhao Lingfeng - Receptor-associated protein 80 (RAP80) is a key component of the BRCA1-A complex and plays an essential role in recruiting this complex to DNA double strand break (DSB) sites to facilitate homologous recombination (HR) repair. The function of RAP80 in DNA damage repair is tightly regulated by post-translational modifications (PTMs). However, the detailed mechanisms by which PTMs modulate RAP80 activity remain to be fully elucidated. Here, we demonstrate that SENP3 dynamically regulates DSB repair by targeting RAP80. Mechanistically, upon DNA damage, RAP80 undergoes SUMOylation and is recruited to DSB sites, promoting subsequent BRCA1 recruitment. SENP3 may facilitate the timely dissociation of RAP80 from DNA damage sites during the later stage, thereby promoting proper repair progression and ensuring timely termination of the DNA damage response. Dysregulation of RAP80 SUMOylation due to depletion impairs HR repair and increases cellular sensitivity to irradiation and chemotherapy drugs. Collectively, our findings identify SENP3 as a key regulator of DNA repair through its dynamic control of RAP80-BRCA1 complex formation and DNA damage repair processes. - Source: PubMed
Publication date: 2026/01/25
Fu JianfengWei MinXu RuidanZheng Xiaofeng