SUMO3 polyclonal antibody
- Known as:
- SUMO3 pab (anti-)
- Catalog number:
- PAB1847
- Product Quantity:
- 100 ug
- Category:
- -
- Supplier:
- Abno
- Gene target:
- SUMO3 polyclonal antibody
Related genes to: SUMO3 polyclonal antibody
- 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 polyclonal antibody
Related articles to: SUMO3 polyclonal antibody
- Pseudorabies virus (PRV), an alphaherpesvirus, establishes lifelong latency in neurons and requires efficient reactivation for pathogenesis. Thymidine kinase (TK), encoded by UL23, is a key virulence factor essential for viral replication in non-dividing cells and for reactivation from latency; however, the regulatory mechanisms governing TK function remain poorly defined. Here, we identify TK as a substrate for small ubiquitin-like modifier (SUMO) modification and investigate its functional significance during PRV infection. We show that TK undergoes endogenous SUMOylation during viral infection is conjugated by SUMO-1, SUMO-2, and SUMO-3, with lysine residues K242 and K267 serving as the principal SUMO acceptor sites. Disruption of these SUMOylation sites does not affect TK stability and kinase activity but markedly alters its subcellular localization by reducing nuclear accumulation. Functionally, SUMOylation of TK is dispensable for viral replication in epithelial PK15 cells but facilitates efficient replication in neuronal N2a cells. Using an in vitro latency/reactivation model, we further show that SUMOylation-deficient TK does not affect the establishment of latent infection but markedly impairs viral reactivation and subsequent productive replication. In a mouse infection model, disruption of TK SUMOylation attenuates PRV pathogenicity, accompanied by reduced viral loads in the brain and milder histopathological lesions. Collectively, our findings demonstrate that SUMOylation regulates nuclear localization and biological function of PRV TK, thereby facilitating efficient neuronal replication, viral reactivation, and pathogenesis. These findings provide new insights into the post-translational regulation of alphaherpesvirus TK and identify TK SUMOylation as a potential target for controlling PRV infection. - Source: PubMed
Publication date: 2026/10/05
Chen XuanLi ChuangXing DongyueSong JingjingLiu YunLiu YuxinHuang QinKuang YuLi XianZhang JinleiZhang YuqiZhang NianzhiBai RulanCheng ChangyongYuan JinTang JunZhang Rui - Protein inhibitor of activated STAT 2 (PIAS2) is highly expressed in various solid tumors. Its precise function as a ferroptosis regulator in hepatocellular carcinoma (HCC) is still unknown. The purpose of this work was to determine whether PIAS2 overexpression attenuates erastin-induced ferroptotic changes and, in turn, is associated with the development of HCC in a manner that correlates with changes in Glutathione Peroxidase 4 (GPX4) protein levels and small ubiquitin-like modifier 3 (SUMO3) modification signals. - Source: PubMed
Cai XiangYe JiangweiFang LinfuDing XiaokunFang ZejunYe Ming - In Arabidopsis, chloroplast protein import relies on the stromal cpHsp70 motor system, whose nucleotide-exchange factor CGE1 is indispensable, yet its regulatory mechanism remains poorly defined. We integrated bioinformatics prediction with in vitro and in vivo SUMOylation assays, biochemical analyses, confocal microscopy, and genetic complementation to elucidate the functional impact of CGE1 SUMOylation in chloroplast development. CGE1 undergoes SUMO3 conjugation, and Lys-214 is required for efficient CGE1 SUMOylation. The SUMOylation-defective variant CGE1 retained stromal localization but caused marked chlorosis of emerging leaves, reduced photosynthetic efficiency, and impaired chloroplast development. Moreover, import of cytosol-synthesized preproteins is compromised in CGE1-complemented plants, accompanied by decreased abundance of TIC40 and TIC110. Loss of SUMOylation simultaneously strengthens the CGE1-cpHsp70-1 and CGE1-TIC40 interactions, and overexpression of either cpHsp70-1 or TIC40 in CGE1-complemented plants restores TIC40 and/or TIC110 levels and the photosynthetic phenotype. In conclusion, these findings reveal that SUMOylation of CGE1 plays an important role in regulating TIC complex abundance and precursor import efficiency through cpHsp70- and TIC40-related routes. This study uncovers a SUMOylation-mediated regulatory layer that fine-tunes chloroplast biogenesis. - Source: PubMed
Publication date: 2026/09/28
Wang CaijuanLiu WenZhao JieLin WenxiongZhang YalinZheng Xiao-TingYang Chengwei - Non-small cell lung cancer (NSCLC) remains a major cause of cancer mortality worldwide, and radioresistance significantly compromises the efficacy of radiotherapy. However, the precise molecular determinants governing NSCLC radiosensitivity remain incompletely defined. Here, we identify SEPT5 as a key regulator of radioresistance, which is aberrantly upregulated in radioresistant NSCLC tissues and cell lines. Mechanistically, reduced expression of the deSUMOylase SENP3 leads to enhanced SUMO3 conjugation of SEPT5 at Lysine 296, thereby protecting it from ubiquitin-proteasome degradation. Accumulated SEPT5 then exerts a dual regulatory effect on the E3 ubiquitin ligase UBE3B. SEPT5 facilitates PCBP3 binding to the 3'-UTR of UBE3B mRNA, stabilizing the transcript and upregulating UBE3B expression. Concurrently, SEPT5 directly recruits UBE3B to promote K48-linked ubiquitination of GSDME at lysines 39 and 120, triggering its proteasomal degradation and suppressing irradiation-induced pyroptosis. Functionally, SEPT5 depletion restores GSDME-dependent pyroptosis and sensitizes NSCLC cells to radiotherapy in vitro and in vivo. More significantly, targeting SEPT5 potentiates the cytotoxic function of tumor-infiltrating CD8 T cells and cooperatively represses NSCLC progression when combined with anti-PD-1. Collectively, these findings define an integrated mechanism in which SUMOylation-dependent stabilization of SEPT5 and UBE3B-mediated GSDME degradation converge to suppress pyroptosis and attenuate antitumor immunity, positioning the SEPT5 regulatory axis as a potential therapeutic vulnerability to overcome radioresistance and enhance the efficacy of immunotherapy. - Source: PubMed
Publication date: 2026/09/15
Wen JunmiaoZheng WangWang BoyanLi HuitingJabbour SalmaShao ChunlinFan MinChen Jiayan - Leaf senescence, the final stage of leaf development, is regulated by complex interplays of intrinsic genetic programs and environmental cues. Throughout their lifetimes, all living organisms encounter various endogenous and environmental challenges, many of which can cause potentially fatal DNA damage. Among these, DNA-protein crosslinks (DPCs) are particularly deleterious, as they obstruct essential processes such as replication and transcription, thereby compromising genome integrity and ultimately leading to premature aging across species. However, the biological significance of DPCs and their repair mechanisms in leaf senescence remains unexplored. Here, we demonstrate that cis-platin (cis-Pt), a potent DPC inducer, accelerates leaf senescence in Arabidopsis. We reveal that Arabidopsis DPC repair factor WSS1A, a WLM/Spr-T metalloprotease, plays a negative role in leaf senescence induced by cis-Pt treatment, darkness, and leaf age. WSS1A forms nuclear condensates via liquid-liquid phase separation both in vitro and in vivo, which is cooperatively driven by its N-terminal segment and intrinsically disordered region. Mechanistically, WSS1A non-covalently interacts with SMALL UBIQUITIN MODIFIER 3 (SUMO3) through its SUMO-interacting motif and is also covalently SUMOylated by SUMO3. Genetic analysis further reveals that WSS1A and SUMO3 act in the same pathway to control cis-Pt-induced leaf senescence. Together, this study establishes a conceptual framework connecting DPC repair and SUMO3-dependent regulation of WSS1A in modulating leaf senescence in Arabidopsis. - Source: PubMed
Park SanghoonOh HyunwooJeong UkcheolLee Jae HoChoi HyeyoungPark HyunsuKim JinkwangKim YongminKwak JunminYoon Yeong SeonLi ZhonghaiLee Jong-ChanWoo Hye Ryun