UBE2F Over-expression Lysate
- Known as:
- UBE2F Over-expression Lysate
- Catalog number:
- LY11302a
- Category:
- -
- Supplier:
- Abgen
- Gene target:
- UBE2F Over-expression Lysate
Related genes to: UBE2F Over-expression Lysate
- Gene:
- UBE2F NIH gene
- Name:
- ubiquitin conjugating enzyme E2 F (putative)
- Previous symbol:
- -
- Synonyms:
- NCE2
- Chromosome:
- 2q37.3
- Locus Type:
- gene with protein product
- Date approved:
- 1999-03-02
- Date modifiied:
- 2016-07-29
Related products to: UBE2F Over-expression Lysate
Related articles to: UBE2F Over-expression Lysate
- Memory CD8 T cells (TMEM) and exhausted CD8 T cells (TEX) are essential for host defense against infection and cancer, yet their therapeutic potential is often limited by insufficient persistence and sustained functional capacity. Strategies to enhance the longevity of both populations remain scarce. Here, we demonstrate that ablation of UBE2F, a neddylation E2 enzyme, induces a resilience program in CD8 T cells that operates across both TMEM and TEX compartments, resulting in improved viral and tumor control. This resilience state is characterized by enhanced self-renewal and survival without perturbing the conventional CD8 T cell differentiation trajectories. Mechanistically, UBE2F deficiency inhibited neddylation of CUL5, leading to accumulation of JUNB and upregulation of IL-2Rβ. The increased IL-2Rβ expression hypersensitizes CD8 T cells to physiological IL-15, thereby conferring the resilience features. Together, these findings identify the UBE2F-CUL5-JUNB-IL-2Rβ axis as a conserved posttranslational mechanism regulating CD8 T cell longevity across memory and exhausted states, providing a novel strategy for enhancing antiviral and antitumor immunity. - Source: PubMed
Publication date: 2026/05/26
Ma XiaonanGuo HenanJia YutingYin NaPeng Min - Succinate dehydrogenase (SDH)-deficient paraganglioma and pheochromocytoma (PPGL) are rare neuroendocrine neoplasms for which no effective targeted therapies currently exist. To uncover potential therapeutic targets, we performed an unbiased CRISPR-Cas9 genetic screen in immortalized mouse chromaffin cells (imCCs) with and without loss. Our screen identified genes that differentially affect cell proliferation in -deficient versus normal imCCs. Subunits of the transcriptional mediator complex emerged as potential tumor suppressors, as their loss selectively promoted growth of -deficient cells. The neddylation pathway, required for ubiquitin-mediated selective protein degradation, plays a critical role in -deficient imCC growth and survival: loss of the neddylation regulator Ube2m led to increased proliferation, while loss of Ube2f suppressed growth of -deficient imCCs. Neddylation inhibitors MLN4924 (Pevonedistat) and HA-9104 reduced UBE2F activity and selectively inhibited growth of -deficient imCCs. This unexpected result highlights the neddylation pathway as a promising druggable vulnerability to be studied in SDH-deficient PPGL. - Source: PubMed
Publication date: 2026/04/28
Al Khazal Fatimah JEmch Michael JCorreia CristinaFavier JudithHawse John RMaher L James - Sepsis is a life-threatening syndrome with dysregulated immune responses and multiple organ dysfunction. However, precise diagnostic biomarkers and effective therapeutic targets for this syndrome are still lacking. Protein ubiquitination modulates inflammatory regulation and immune cell function, but the specific immune cell subsets that drive ubiquitination-associated immune dysregulation in human sepsis have not been clearly identified. - Source: PubMed
Publication date: 2026/04/22
Li ChengHan YimanZheng ZengluHuang ChengyaLiu ZhiyunZhou JianwenYang RuiWu Jingxiang - Natural killer (NK) cells are promising effectors for cancer immunotherapy, but their efficacy is limited by immunosuppressive tumor microenvironments. To uncover strategies for enhancing NK cell function, we establish a CRISPR loss-of-function screening platform for primary human NK cells by combining BaEVRless-pseudotyped lentiviral transduction of sgRNA libraries with Cas9 protein electroporation. This platform enables genome-scale interrogation of gene function in non-transformed NK cells. Kinome-focused and genome-wide screens identify key regulators of NK cell proliferation, cytotoxicity, and resistance to prostaglandin E (PGE)-mediated suppression. STK17B deletion enhances NK cell expansion, while loss of CCDC53 boosts degranulation and cytotoxicity. We also uncover the CRL5 complex-including RNF7, UBE2F, and CISH-as critical inhibitors of IL-2 signaling and effector function under PGE stress. These findings establish a scalable platform for CRISPR-based functional genomics in primary NK cells and reveal engineering targets to enhance NK cell persistence and efficacy in tumor microenvironments. - Source: PubMed
Publication date: 2026/04/15
Nguyen Quoc VietLan Yi-JunChang Jason Cheng-YuShih Hsin-AnFaustine JeniferChen Cheng-ChiehHo Shu-YuCheng Ching-WenChao Tsu-LanLin Steven - Pseudorabies virus (PRV) is an important swine herpesvirus that causes fatal encephalitis in newborn piglets and severe reproductive failure in pregnant sows, resulting in enormous economic losses in the pig industry worldwide. It has broad cell tropisms with the capability to infect a wide range of animals, including humans, thus posing a potential threat to human health. Neddylation is an important protein posttranslational modification that is catalyzed by an E1-E2-E3 enzyme cascade to covalently conjugate the ubiquitin-like molecule neural precursor cell expressed developmentally downregulated 8 (NEDD8) to substrate proteins. It has been demonstrated to play a key role in regulating numerous important biological processes, including cell proliferation, gene expression, signal transduction, and viral infection. However, the specific function of the neddylation pathway during PRV infection remains largely unknown. In the work described here, we identified a critically important role for neddylation in PRV replication by utilizing short hairpin RNA (shRNA)-mediated depletion of NEDD8 or the NEDD8-activating enzyme E1 subunit 1 (NAE1). Through systematic investigation of E2-E3 neddylation partners, we further demonstrated that silencing of the ubiquitin conjugating enzyme E2 F (UBE2F)-RING-box protein 2 (RBX2) axis significantly decreased PRV replication. Furthermore, knockdown of the neddylation substrate Cullin5 (CUL5) or pharmacological inhibition of CUL5 neddylation significantly attenuated PRV replication. Cumulatively, these findings demonstrate that the UBE2F-RBX2-mediated neddylation of CUL5 facilitates PRV replication. This study provides a new theoretical basis for in-depth understanding of PRV-host interaction and reveals neddylation as a novel target for antiviral strategies against PRV. - Source: PubMed
Publication date: 2025/12/30
Zheng ZhiyuanZhao FeiZhao SenhongBai YaningShi LunwenZhu BinbinHuang XiaoboZheng YiZhao QinWen YipingWu RuiDu SenyanCao SanjieYan QiguiXu ZhiwenTibbetts Scott AWang Yiping