Ask about this productRelated genes to: SUMO1 protein
- Gene:
- SUMO1 NIH gene
- Name:
- small ubiquitin like modifier 1
- Previous symbol:
- UBL1
- Synonyms:
- PIC1, GMP1, SMT3C, SUMO-1, SMT3H3, OFC10
- Chromosome:
- 2q33.1
- Locus Type:
- gene with protein product
- Date approved:
- 1996-06-04
- Date modifiied:
- 2019-02-18
Related products to: SUMO1 protein
Related articles to: SUMO1 protein
- Simian immunodeficiency viruses (SIVs) have crossed from apes to humans at least four times, but only one event gave rise to the AIDS pandemic. The host barriers that pandemic HIV-1 group M () strains overcame to spread efficiently in humans remain poorly understood. To identify such barriers, we performed CRISPR-Cas9 screens driven by the replication efficiency of SIVcpz, the chimpanzee precursor of HIV-1. Guide RNA libraries targeting more than 500 human genes encoding potential antiviral factors were inserted into the replication-competent SIVcpz MB897 molecular clone, which is phylogenetically closely related to HIV-1 group M strains. Propagation in Cas9-expressing human SupT1 T cells significantly enriched for sgRNAs targeting and . These hits only partially overlapped with those identified in analogous HIV-1-based screens, indicating virus-specific restriction profiles. Functional analyses confirmed that IFITM2 (interferon-induced transmembrane protein 2), PCED1B (PC-esterase domain-containing protein 1B), MEFV (Mediterranean fever protein, pyrin/TRIM20), and AXIN1 (Axis inhibition protein 1) restrict replication of the analyzed SIVcpz strains but not HIV-1 group M strains in primary human CD4 T cells. These findings reveal previously unrecognized host factors that limit SIVcpz replication in human cells and highlight barriers that at least some HIV-1 group M strains overcame during adaptation for pandemic spread. - Source: PubMed
Publication date: 2026/05/07
Xie QinyaWang QingxingNoettger SabrinaGosálbez GuillermoBetzler Annika CVolcic MetaKmiec DorotaKrebs StefanGraf AlexanderGülensoy DilaWeidinger GilbertSparrer Konstantin M JKirchhoff Frank - SUMOylation may be involved in preeclampsia (PE) progression. We aimed to investigate the roles of SUMOylation in PE and its underlying mechanism using animal and cell models. A rat PE model was established by dexamethasone (DEX) treatment from pregnancy day 7.5-17.5. HTR8 and BeWo trophoblasts were used as cell models. Placental RNA-seq analysis coupled with Western blotting showed upregulated SUMOylation in placentas of DEX-treated rats. SUMOylation inhibitor TAK-981 treatment robustly alleviated PE-like features including reduced blood pressure and improved renal injury, fetal weight, spiral artery remodeling and placental blood flow in DEX-treated rats. DEX increased SUMOylation in HTR8 and BeWo cells. TAK-981 reversed DEX-induced dysfunction in HTR8 and BeWo cells, such as migration, invasion and syncytialization. Mass spectrum analysis of SUMO1 immunoprecipitation coupled with functional validation showed that SUMOylated proteins related to oxidative stress caused by DEX were reversed by TAK-981 in cultured trophoblasts. TAK-981 mitigated placental oxidative stress in DEX-treated rats. GEO database combined with Western blotting showed upregulated SUMOylation in human placentas with PE. Our findings indicate that protein SUMOylation is one of the key events in PE, particularly in that associated with high glucocorticoid exposure. Targeting placental SUMOylation might be a promising therapeutic strategy for PE. - Source: PubMed
Publication date: 2026/04/11
Xiao ShuZhang YouyiTang ZhengshanChen CaiyunGuo DeweiLong JingNi Xin - Mitochondrial damage and subsequent aberrant mitophagy are critical drivers of alveolar simplification in bronchopulmonary dysplasia (BPD). E26 transformation specific-1 (ETS1) is a transcription factor whose role in BPD and its regulation of mitophagy have not been fully investigated. This study aims to explore the role of ETS1 in mitophagy in BPD and its underlying molecular mechanisms. Using hyperoxia-induced BPD models in cells and mice, we found that ETS1 overexpression simplified alveolar structure, reduced alveolar number, inhibited mitophagy, improved cell viability and mitochondrial damage. Mechanistically, EST1 promoted the transcription of SENP2. After SENP2 removed the SUMO1 modification from FUNDC1, the binding site of HSPA8 was exposed, thereby promoting the degradation of FUNDC1. In BPD mice, ETS1 overexpression alleviated lung injury and inhibited mitophagy, while SENP2 knockdown reversed these effects. In conclusion, ETS1, as a novel transcriptional hub, maintained mitochondrial homeostasis by coordinating the deSUMOylation-coupled FUNDC1 degradation pathway. ETS1 blocked mitochondrial damage-induced mitophagy by targeting the SENP2/HSPA8/FUNDC1 axis, providing a promising strategy for the treatment of BPD. - Source: PubMed
Publication date: 2026/04/30
Yang MinYang QinglanMeng YanniZhang JiyanLi Shuangjie - Gram-negative bacteria use a plethora of virulence factors to infect eukaryotic cells. CE-clan protease-related virulence factors were reported to act as deubiquitinases/ubiquitin-like specific proteases. Some have an additional acetyl-transferase activity. The molecular mechanisms underlying this dual activity and the physiological consequences are only marginally understood. Here, we report crystal structures for the Simkania negevensis virulence factor SnCE1 in apo-states and in complex with SUMO1. We confirm SnCE1 acting as an efficient deSUMOylase and discover an intrinsic autoacetyltransferase activity. Acetylation impairs SnCE1 tetramer formation structurally being incompatible with SUMO1 binding. We provide a model for regulation of SnCE1-mediated virulence by lysine acetylation modulating autoproteolytic processing and its subcellular distribution in the host cell. SnCE1 localizes to the endoplasmic reticulum in human cells and increases fragmentation of mitochondria. Our data provide mechanistic insights into how lysine acetylation of virulence factors is used to reprogram virulence adjusting it to the host cells' metabolic state. - Source: PubMed
Publication date: 2026/04/27
Schmöker OleGirbardt BrittaSchulze SabrinaPalm Gottfried JBerndt LeonaHoppen JensKara NilüferSchöps XeniaAl-Abdulla RubaGarz KlaraJunker HeikeWolfgramm SophieSteil LeifHentschker ChristianSchoknecht KatrinMayer Lea-MariaSpeth LeonieLachmayer VanessaDörr MarkKemnitz StefanMüller StefanLackmann Jan-WilmKrüger MarcusHofmann KayBornscheuer Uwe TVölker UweKrüger ElkeKozjak-Pavlovic VeraLammers Michael - Perturbation of macrophage homeostasis is a key mechanism of airway inflammation in asthma. Ubiquitin conjugating enzyme E2 I (UBE2I), a SUMO E2 conjugating enzyme involved in macrophage M2 polarization, has an unclear role in asthma. - Source: PubMed
Publication date: 2026/04/25
Lin HongYu SijiaLi XiaowenYu LianyuChen XinyanPang YunyaoLv RourouDai BingZhou QianlanShan Lishen