Ask about this productRelated genes to: UFM1 antibody
- Gene:
- UFM1 NIH gene
- Name:
- ubiquitin fold modifier 1
- Previous symbol:
- C13orf20
- Synonyms:
- bA131P10.1
- Chromosome:
- 13q13.3
- Locus Type:
- gene with protein product
- Date approved:
- 2004-04-16
- Date modifiied:
- 2016-07-06
Related products to: UFM1 antibody
Related articles to: UFM1 antibody
- Targeting autophagy initiation represents a promising strategy to disrupt the metabolic resilience of cancer cells. In this study, we identified ATI-1 as a novel small-molecule inhibitor that selectively blocks the early stages of autophagosome formation. Importantly, we discovered that ATI-1-mediated de novo inhibition of autophagy initiation leads to a synergistic surge in cell death under nutrient-deprived conditions, revealing a critical, context-specific vulnerability in autophagy-dependent malignancies. Mechanistically, ATI-1 appears to target valosin-containing protein (VCP/p97) and disrupt its interaction with the UFM1-specific E3 ligase UFL1. This disruption may promote the polyubiquitination and subsequent degradation of Beclin1, thereby contributing to the inhibition of autophagy initiation. Furthermore, ATI-1 demonstrates potent antitumor efficacy in xenograft models with minimal overt toxicity. This work collectively suggests that the VCP-UFL1-Beclin1 axis may represent a potentially targetable node in autophagy regulation, and identifies ATI-1 as a potential small-molecule modulator of this pathway, thereby providing a promising therapeutic lead for cancer treatment. - Source: PubMed
Publication date: 2026/04/25
Liu TongZhao MinGao JingLiu JieZhang Jifa - Chromosomal instability (CIN) is a prevalent form of genomic instability in prostate cancer (PCa). However, its molecular mechanisms remain inadequately understood. This study demonstrates that reduced expression of UFM1-ligase 1 (UFL1) is commonly observed in PCa and correlates with elevated CIN rates. UFL1 deficiency results in severe mitotic defects, errors in chromosome segregation, and aneuploidy, thereby promoting malignant transformation. Mechanistically, UFL1 interacts with RNF20 and catalyzes its UFMylation, which enhances RNF20 binding to CEP192, facilitating its centrosomal localization and supporting mitotic spindle assembly. Additionally, downregulation of the microphthalmia-associated transcription factor (MITF) exacerbates PCa aggressiveness by suppressing UFL1 expression. These findings identify the MITF-UFL1-RNF20 axis as a critical regulator of spindle integrity and a potential therapeutic target in PCa. - Source: PubMed
Publication date: 2026/04/20
Li JiminYang FangZhang XiaoXu LiangfeiZheng HuiLiu LiuWan XinXu TaoJiang GuanminWang Hao - Oral squamous cell carcinoma (OSCC) is highly invasive malignancy with limited effective therapeutic strategies. Ubiquitin-fold modifier 1 (UFM1) is a ubiquitin-like molecule that has been implicated in several cancers; however, its role in ferroptosis within OSCC remains unclear. In this study, UFM1 was demonstrated to be upregulated in OSCC. UFM1 depletion suppressed proliferation and dissemination of OSCC cells and induced ferroptosis characterized by increased lipid peroxidation and Fe accumulation. Mechanically, UFM1 deficiency significantly reduced SLC7A11 levels and sensitized cells to oxidative stress. Reintroduction of SLC7A11 rescued ferroptosis and restored cell survival in UFM1-deficient cells. , UFM1 depletion significantly inhibited tumor growth, reduced SLC7A11 expression, and increased lipid oxidation, as indicated by 4-hydroxynonenal (4-HNE) immunohistochemical staining. These findings suggest that UFM1 protects OSCC from ferroptosis by stabilizing SLC7A11 protein via UFMylation, thereby preventing its proteasomal degradation. - Source: PubMed
Publication date: 2026/03/25
Li GangYang HongweiGuo Jing - Atherosclerosis is a chronic and progressive inflammatory disease that can lead to adverse cardiovascular and cerebrovascular events. Phenotypic switching of vascular smooth muscle cells (VSMCs) plays a pivotal role in its development and progression, but the upstream regulatory mechanisms remain incompletely defined. Here, we identify ubiquitin-fold modifier 1 (UFM1), a ubiquitin-like protein, as a critical regulator of VSMCs plasticity and atherogenesis. In VSMCs stimulated with oxidized low-density lipoprotein (ox-LDL), UFM1 overexpression markedly attenuated phenotypic switching, restoring contractile features and suppressing synthetic activation, accompanied by reduced proliferation and migration. In contrast, UFM1 knockdown further exacerbated these phenotypic alterations. In ApoE mice, adeno-associated virus (AAV)-mediated UFM1 overexpression attenuated VSMCs phenotypic transition and Ki67-positive cell proliferation and significantly reduced atherosclerotic plaque burden. Transcriptomic analyses revealed the phosphoinositide 3-kinase (PI3K)-protein kinase B (AKT) and mitogen-activated protein kinase (MAPK) pathways as downstream candidates, and subsequent pharmacological inhibition experiments confirmed that the PI3K-AKT signaling pathway is the primary mediator of the protective effects of UFM1. Mechanistically, UFM1 limited AKT phosphorylation, thereby restraining VSMCs dedifferentiation and lesion development. Collectively, these findings highlight the UFM1-AKT axis as a promising therapeutic target for atherosclerotic cardiovascular disease. - Source: PubMed
Publication date: 2026/04/12
Zhang QianruAikebaier MirenuerHu YefanMa XiaowenMao ZimingZhu JingLiu YanChen Fengling - Ufmylation is a newly identified ubiquitin-like modification of histones and plays important roles in DNA-related processes. Dissecting histone ufmylation pathways necessitates the use of chemically defined proteins to assign their structural and functional consequences; however, the preparation of ufmylated histones has not yet been reported. Here, we report the chemical synthesis of ufmylated histones and their analogs through semisynthetic strategies integrating chemoenzymatic C-terminal hydrazinolysis of ubiquitin-fold modifier 1 (UFM1) and auxiliary-mediated formation of an isopeptide bond. The results indicated that the E1-mediated activation of UFM1 can be hijacked by nucleophilic reagents, forming the full-length UFM1 hydrazide that can be readily installed onto histones via auxiliary-mediated ligations. The synthetic histones enabled us to reveal that the two known UFM1-specific proteases 1 and 2 (UfSP1 and UfSP2) cannot efficiently cleave H4 ufmylation at Lys31 (H4K31UFM1) in the nucleosome context. Furthermore, cryo-electron microscopy (cryo-EM) analysis of the H4K31UFM1-nucleosome suggested that the steric hindrance of the nucleosome around the isopeptide bond might be one of the potential reasons for the weak activities of UfSPs. Collectively, we developed practical strategies for the efficient generation of ufmylated histones and exemplified their use in biochemical and structural studies related to histone ufmylation. - Source: PubMed
Publication date: 2026/04/11
Liu XinChen CongLi FangLiu XiaotongLu ChengpiaoLi YuanpengPeng ShuaiXu HongruiTian ChanglinXu GuoqiangLi Jia-Bin