SUMO3
- Known as:
- SUMO3
- Catalog number:
- 000251A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- SUMO3
Related genes to: SUMO3
- Gene:
- SUMO3 NIH gene
- Name:
- small ubiquitin like modifier 3
- Previous symbol:
- SMT3H1
- Synonyms:
- SMT3A
- Chromosome:
- 21q22.3
- Locus Type:
- gene with protein product
- Date approved:
- 1997-01-29
- Date modifiied:
- 2019-02-18
Related products to: SUMO3
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- Small ubiquitin-related modifiers (SUMOs) are covalently conjugated onto the proteome and serve as signaling molecules in many aspects of eukaryotic cell biology, from and to . The conjugatable SUMO variants, SUMO1 and the almost identical SUMO2 and SUMO3 (designated SUMO2/3), are processed by an E1(SAE1:SAE2)-E2(UBC9)-E3 enzyme cascade to produce SUMO-modified proteins. The prerogative of the SUMO biology field is to identify and study the specific proteins undergoing SUMOylation, which grants us insights into the biological pathway of interest. This protocol was developed using the human osteosarcoma cell line U2OS to enable the investigation of SUMO conjugates in mitosis, the cell division phase of the cell cycle. We enrich the cell population for mitotic cells, which are isolated and subjected to stringent lysis conditions involving a high concentration of SDS and DTT in RIPA buffer, to promote complete protein denaturation. The lysates in high SDS RIPA buffer are diluted to reduce the overall SDS concentration and undergo conventional immunoprecipitation using SUMO1- or SUMO2/3-specific antibodies bound to protein A/G agarose beads. The samples are then compatible with downstream readouts such as western blots and mass spectrometry. This protocol detects endogenous SUMOylated proteins and avoids exogenous SUMO overexpression, which can alter SUMO conjugate formation. Furthermore, this denaturing protocol ensures only SUMOylated proteins are immunoprecipitated, and not their interactors. Key features • Purifies endogenous SUMO-modified proteins by building on Becker et al. [1]. • Enriches and isolates cells in mitosis using nocodazole and mitotic shake-off. • 1% SDS RIPA lysis promotes robust denaturation ahead of SUMO-specific immunoprecipitation. • Compatible with downstream readouts such as western blots and mass spectrometry. - Source: PubMed
Publication date: 2026/04/05
Walker Alexandra KLanz Alexander JMorris Joanna R - Dysfunction of SUMOylation is closely associated with various diseases, yet its role in lung ischemia-reperfusion injury (LIRI) remains poorly understood. This study used quantitative real-time PCR and Western blot to assess the expression levels of small ubiquitin-like modifier 3 (SUMO3) and heat shock protein 70 (HSP70). The stability of HSP70 and protein-protein interactions were also detected. Flow cytometry and terminal deoxynucleotidyl transferase-mediated dUTP nick-end labeling staining were performed to detect cell apoptosis. Immunofluorescence was applied to assess the expression levels of Bip, phosphorylated protein kinase r-like endoplasmic reticulum kinase, and phosphorylated inositol-requiring enzyme 1. Enzyme-linked immunosorbent assay kits were used to measure the content of cytokines. This study found that SUMO3 was down-regulated in both the hypoxia/reoxygenation-induced cell model and the in vivo ischemia-reperfusion injury-mediated lung injury model. SUMO3 up-regulation effectively promoted cell growth in vitro and attenuated lung injury in vivo. Mechanistically, SUMO3 interacts with HSP70 and promotes its SUMOylation, thereby stabilizing HSP70 protein and subsequently suppressing endoplasmic reticulum (ER) stress. Knockdown of HSP70 reversed the beneficial effects induced by SUMO3 up-regulation, such as inhibiting cell growth and activating ER stress in vitro and aggravating lung injury and enhancing inflammatory response in vivo. These findings demonstrate that SUMO3 exerts a protective role in LIRI progression by stabilizing HSP70 and inhibiting ER stress, providing a potential therapeutic strategy for LIRI treatment. - Source: PubMed
Publication date: 2026/03/23
Li AoLi ChunkeLi HuLiu YuweiDing ZhiTan Jing - Flaviviridae viruses constitute formidable zoonotic agents with substantial global health and economic ramifications, attributable to their adeptness at circumventing host immune surveillance and establishing persistent infections across human and animal populations. Despite their pervasive impact, broadly effective antiviral strategies remain elusive. Emerging studies underscore the pivotal role of RNA modifications, particularly 5-methylcytosine (m5C), in fine-tuning host-pathogen interactions. Expanding upon prior evidence linking NSUN2-mediated m5C deposition to Classical swine fever virus (CSFV, Pestivirus of Flaviviridae) persistence, the present study demonstrates that Japanese encephalitis virus (JEV, Flavivirus of Flaviviridae) similarly commandeers host epitranscriptomic machinery. Specifically, JEV-encoded RNA-dependent RNA polymerase (RdRp) engages the SAE1 to induce SUMO3/4-mediated stabilization of NSUN2. Elevated NSUN2 promotes m5C methylation of Cebpd mRNA, expediting transcript degradation and dampening cGAS-STING-driven antiviral signaling. This regulatory cascade facilitates viral replication and persistence. This regulatory axis supports sustained viral replication and persistence. Notably, a homologous mechanism is operative in Orthomyxoviridae infection, indicating evolutionary convergence on NSUN2 as a proviral effector. Overall, these unprecedented findings define a conserved RdRp-SAE1-NSUN2-CEBPD axis as a key epitranscriptomic immune evasion strategy and nominate m5C methyltransferases as tractable targets for host-directed, broad-spectrum antiviral therapy. - Source: PubMed
Publication date: 2025/12/04
Chen JingZhong Lin HanChen Jin XiaSong Hui XinZou Lin KeBi Xiao QingZhao Bing QianLi Mei ZhenLi KunWang KangYang Jia JunCui JinWang LiZhou Bin - The centromere is a specialized domain that facilitates chromosome segregation during mitosis and serves as the site of kinetochore formation. KINETOCHORE NULL2 (αKNL2) is essential for the recognition and loading of the centromeric histone H3 variant CENH3 at centromeres. A yeast two-hybrid screen for αKNL2 interactors identified components of the SUMOylation pathway. However, the role of αKNL2 SUMOylation in Arabidopsis has not yet been determined. In this study, we demonstrated that the C-terminal region of αKNL2 (designated αKNL2-C) interacts with small ubiquitin-like modifier 3 (SUMO3) and ULP1d, as shown by bimolecular fluorescence complementation and co-immunoprecipitation assays. Bioinformatic and functional analyses of αKNL2-C identified three SUMOylation sites and two SUMO-interacting motifs, which were shown to be critical for growth, fertility, and chromosome alignment. Of the three SUMOylation sites, Lys474 and Lys511 are the most critical for the centromeric localization of αKNL2, underscoring the importance of αKNL2 SUMOylation for its function. Additionally, both in vitro and in vivo assays showed that αKNL2-C undergoes SUMOylation by SUMO1 or SUMO3. The Arabidopsis SUMO protease mutant ulp1d-2 exhibits a mild accumulation of SUMOylated αKNL2. We further showed that SUMOylation of αKNL2 promotes its binding to CENH3 and controls protein stability. Our findings demonstrate that C-terminal SUMOylation of αKNL2 is crucial for its centromeric localization, interaction with CENH3, and kinetochore assembly, emphasizing the significance of post-translational modifications in chromosome segregation and cell division in plants. - Source: PubMed
Publication date: 2025/11/19
Kalidass ManikandanVaculíková JitkaChandra Jothipriya RamakrishnanKrálová BarboraJarubula Venkata GaneshKara Öztürk Sevim DDemidov DmitriSchubert VeitPotesil DavidPalecek Jan JLermontova Inna - SENP3, a member of the sentrin-specific protease family, plays a pivotal role in lipid metabolism and the pathogenesis of fatty liver disease by regulating the dynamic process of SUMOylation. It has previously been demonstrated that SREBP2 is SUMOylated. However, the function and regulatory mechanism of SENP3-mediated SREBP2 de-SUMOylation in hepatocyte steatosis is unclear. Bioinformatic analysis (proteomes from whole cell extract and nuclear extraction, integrated transcriptomes, RNA sequence) SENP3-driven SREBP2 de-SUMOylation in lipid metabolism; Oil red O, nuclear and cytoplasmic extraction, western blot and immunofluorescence suggest SENP3 vitally contributes to hepatocyte steatosis; NLS predictions, CO-IP, co-transfection of plasmids, confocal microscopy indicates nuclear SENP3 associates with SREBP2 to promote its nuclear translocation; molecular docking and mutation assay confirmed SENP3 is responsible for de-SUMOylation SREBP2 at R576. Treatment with OA increased the level of both SENP3 and its nuclear fraction in HepG2 cells. Interfering with the SUMOylation and deSUMOylation cycle induced hepatocyte steatosis by overexpressing SENP3 and using a SUMO inhibitor, GA. Mechanistically, it is observed that the co-localization between SREBP2 and SENP3 is increased. SENP3 is responsible for de-SUMOylation SREBP2 at R576. Moreover, SENP3-mediated de-SUMOylation may also decrease ZMIZ1-ligated SUMO3 binding to SREBP2 at K464 in the nucleus. RNA interference of SREBP2 cannot reverse SENP3-overexpressed cell steatosis under fatty acid treatment. Expression of SREBP2 in vitro could upregulate the nuclear locations of CCTα binding to DNA without altering the active forms. Our findings demonstrate that de-SUMOylation is an important regulatory mechanism that governs the lipid accumulation of SREBP2 in mammalian cells. Also, the critical role of the de-SUMOylation of SREBP2 by SENP3 to exacerbate steatosis may be a potential therapeutic target for metabolic diseases like MAFLD/MASH. - Source: PubMed
Tang QianyuPeng WenjingJiang XiaohuaHu YangChen LinxiFu Nian