Ask about this productRelated genes to: LOC51035 antibody
- Gene:
- UBXN1 NIH gene
- Name:
- UBX domain protein 1
- Previous symbol:
- -
- Synonyms:
- LOC51035, 2B28, UBXD10, SAKS1
- Chromosome:
- 11q12.3
- Locus Type:
- gene with protein product
- Date approved:
- 2008-07-25
- Date modifiied:
- 2016-10-05
Related products to: LOC51035 antibody
Related articles to: LOC51035 antibody
- Colorectal cancer (CRC) is a common malignancy in clinical practice, and its treatment is greatly challenged by tumor heterogeneity. The most prominent features of CRC heterogeneity are differences in metabolic states and genomic instability, which ultimately lead to unfavorable clinical outcomes. Based on this, the present study aimed to investigate the association between metabolic reprogramming and copy number variation (CNV) in CRC using single-cell datasets. By integrating four publicly available single-cell RNA sequencing datasets, a comprehensive single-cell atlas of CRC was constructed. Subsequently, epithelial cells were specifically analyzed, and consensus non-negative matrix factorization (cNMF) was applied to identify six gene expression programs, covering functional modules such as cell cycle, metabolism, inflammatory stress, and immune interaction. Genomic instability was assessed using the inference of copy number variations (InferCNV) analytical tool, which identified malignant epithelial cells characterized by large-scale CNVs. Meanwhile, metabolic pathway activity at the single-cell level was evaluated using the area under the curve cell (AUCell) method, and predictive performance was further assessed using machine learning algorithms. The results demonstrated that metabolic features could effectively predict the malignant state defined by CNVs, achieving an area under the curve (AUC) of 0.985, with protein metabolism and TP53-related pathways contributing most significantly. Further integrative analysis identified 13 metabolism-related genes associated with clinical prognosis, among which UBXN1 was identified as a central node in the protein-protein interaction network. Functional analysis of UBXN1 revealed that it suppresses the NF-κB signaling pathway, thereby regulating the malignant phenotype of CRC cells. In conclusion, this study systematically elucidates the critical link between metabolic features and genomic instability in CRC, suggesting that UBXN1 may serve as a potential therapeutic target. - Source: PubMed
Publication date: 2026/03/25
Qian LongLi ZiyiYang TangtangXia ShashaJin LeiZhu ChengyuJing WenshanWang YueYe YunShen YiLi LixiangPeng HuiYu Qingsheng - In PINK1 (PTEN induced kinase 1)/PRKN (Parkin)-mediated mitophagy, the rupture of the outer mitochondrial membrane (OMM) emerges as a crucial event required for efficient mitochondrial clearance. Mechanistically, OMM rupture exposes inner mitochondrial membrane (IMM) mitophagy receptors, facilitating subsequent autophagic removal. Despite the important role of OMM rupture in mitophagy, the underlying mechanism remains elusive and technically difficult to monitor. In a recent study, we developed a novel fluorescent biosensor to directly visualize OMM rupture. This technique enables temporal and spatial characterization of OMM rupture and provides a powerful platform to dissect the underlying mechanism. Using this tool, we revealed that VCP (valosin containing protein) and its recruitment factors are required for OMM rupture, suggesting that VCP-dependent remodeling of the OMM proteome primes the rupture of OMM during mitophagy. : ARIH1, Ariadne RBR E3 ubiquitin protein Ligase 1; AMFR, autocrine motility factor receptor; ANKRD13A, ankyrin repeat domain-containing protein 13 A; FUNDC1, FUN14 domain containing 1; OA, oligomycin and antimycin; CID, chemical-induced dimerization; IMM, nner mitochondrial membrane; LC3, microtubule-associated protein 1 light chain 3; MUL1, mitochondrial E3 ubiquitin protein ligase 1; NIX, BCL2 interacting protein 3 like; OMM, outer mitochondrial membrane; UBXN1, ubiquitin regulatory X domain-containing protein 1; UBXN6, ubiquitin regulatory X domain-containing protein 6; VCP, valosin-containing protein; WIPI2, WD repeat domain phosphoinositide interacting protein 2. - Source: PubMed
Publication date: 2026/02/13
Chu Wei-HuaChiang Wei-Chung - Deubiquitinating enzymes (DUBs) are a class of biological macromolecules with molecular weights ranging from 30 to 150 kDa that play extensive roles in tumor initiation and progression. However, their implications in sorafenib resistance in liver cancer remain incompletely understood. In this study, we identified sorafenib resistance-associated DUBs through weighted gene co-expression network analysis and differential expression profiling. Subsequently, we developed a DUB-based predictive model for liver cancer resistance, designated ResiDUBs, using multivariate Cox regression analysis. This model was employed to assess drug resistance and prognostic outcomes. The ResiDUBs model-constructed based on five DUBs (OTUB1, USP32, USP48, USP49, and UBXN1)-stratified patients into high- and low-risk groups. Patients in the high-risk group exhibited significantly greater sorafenib resistance, poorer prognosis, and hyperactivation of the PI3K/AKT signaling pathway. Multi omics analyses, including single-cell RNA sequencing, spatial transcriptomics, and bulk RNA sequencing, consistently identified UBXN1 as the most prominent resistance-associated gene within the ResiDUBs signature. UBXN1 expression was markedly upregulated in treatment-resistant tumors. Knockdown of UBXN1 sensitizes liver cancer cells to sorafenib and inhibits PI3K/AKT pathway activity. Conversely, overexpression of UBXN1 increases cellular resistance to sorafenib, activates the PI3K/AKT pathway, and induces macrophage polarization toward the M2 phenotype. In vivo experiments further demonstrate that UBXN1 knockdown enhances the sensitivity of liver cancer cells to sorafenib and significantly reduces PI3K/AKT pathway activity. Our findings suggest that targeting UBXN1 may represent a promising therapeutic strategy to overcome sorafenib resistance in liver cancer. - Source: PubMed
Publication date: 2026/01/27
Li ManqiXie YuxinWei JinruiWu Lichuan - Through its various roles in protein quality control, membrane dynamics, and cellular survival pathways, the AAA+ ATPase p97/valosin-containing protein emerges as a significant regulator of mitochondrial homeosta sis. This review comprehensively examines the multifaceted functions of p97 in mitochondrial biology, spanning from mitochondria-associated degradation to newly discovered functions in organellar cross-talk and disease pathogenesis. Underlying its cellular importance, p97 mutations are found in amyotrophic lateral sclerosis and frontotemporal dementia. To elucidate its mechanistic contribution to these processes, we provide a detailed table (Table 1) listing all known mitochondrial Cdc48/p97 substrates and associ ated proteins, categorized by their respective pathways. Recruitment to most of these substrates occurs by specialized adaptors, including Doa1/phospholipase A-2-activating protein, UBXD8, and UBXN1. p97 orchestrates the extraction and proteasomal degradation of outer mitochondrial membrane proteins, which are essential for maintaining mitochondrial integrity. For example, by controlling the turnover of fusion factors MFN1/2 and fission machinery, p97 regulates mitochondrial dynamics. p97 also governs apoptotic signaling through the regulated degradation of anti-apoptotic factors, such as myeloid cell leukemia-1 and VDAC, thereby modulating mitochondrial permeability. In mitophagy, p97 enables the clearance of damaged organelles by extracting ubiquitinated substrates and recruiting autophagy machinery. Beyond proteolysis, p97 facilitates recycling of endoplasmic reticulum-mitochondria contact sites through regulation of UBXD8-dependent lipid metabolism. Recent discoveries have revealed p97's involvement in pathogen host interactions and circular RNA-mediated regulation, thereby expanding our understanding of its cellular functions. The emerging picture positions p97 as an integrative hub co-ordinating mitochondrial protein homeostasis, organellar dynamics, and cell fate decisions, with therapeutic potential for metabolic and neurodegenerative disorders. - Source: PubMed
Ram JonathanGlickman Michael H - Circadian dysregulation has been shown to be associated with the progression of pancreatic cancer (PC). However, the circadian machinery comprises numerous circadian rhythm-related genes (CRRGs), whose roles in tumor biology remain unclear. - Source: PubMed
Publication date: 2025/11/26
Cheng ZhiyuanYu ChutingQuan BinZhou KenaHe ChongxinShen ShuangjunWu XiaowanYu GuoLiu LehengGuo ZihaoSun HaoranWan RongZhao KaiLu ZhanjunJiang Weiliang