Ask about this productRelated genes to: ZNF143 antibody
- Gene:
- ZNF143 NIH gene
- Name:
- zinc finger protein 143
- Previous symbol:
- -
- Synonyms:
- SBF, pHZ-1, STAF
- Chromosome:
- 11p15.4
- Locus Type:
- gene with protein product
- Date approved:
- 1993-06-07
- Date modifiied:
- 2014-11-18
Related products to: ZNF143 antibody
Related articles to: ZNF143 antibody
- Enhancers regulate genes over long genomic distances by physically looping to interact with promoters, a process highly dependent on specific protein recruitment and local histone modifications. We identified 1399, 1394, and 4063 enhancer-associated chromatin loops in GM12878, K562, and HepG2 cell lines, respectively, and found that dual-function proteins, characterized by both activating and repressing activities, preferentially localized at loop-anchored enhancers. Although protein co-localization patterns varied among cell types, CTCF, RAD21, SMC3, and ZNF143 consistently co-localized with one another at these enhancers. Furthermore, enhancer-associated loops localized primarily to the A compartment. Enhancers anchored in A-A loops showed greater enrichment of H3K4me1, H3K4me2, H3K9ac, and H3K27ac than those anchored in B-B loops. However, in K562 cells, enhancers anchored in B-B loops exhibited minor changes in active histone modification enrichment compared to their A-A counterparts, and even showed higher proportions of H3K4me2 and H3K9ac enrichment for enhancer-promoter loops. Nevertheless, across all three cell lines, A-A enhancer-promoter loops with both active anchors exhibited significantly higher target gene expression than other A-A loops and B-B loops. Our study suggests that enhancer-associated loop formation correlates with dual-function protein co-localization and active histone modification enrichment, which may collectively contribute to target gene transcription. - Source: PubMed
Publication date: 2026/08/07
Sheng WeiNie Yumin - Metabolically dysfunction-associated steatotic liver disease (MASLD), a globally prevalent metabolic condition, is increasingly linked to impaired mitophagy. However, its regulatory mechanisms in MASLD are not fully elucidated. This study investigated the role of Zinc finger protein 143 (ZNF143) in regulating hepatocyte mitophagy during MASLD development and the mechanisms involved. We employed two complementary MASLD models: (1) C57BL/6J mice fed a high-fat diet (HFD) for 16 weeks and (2) Huh-7 cells exposed to free fatty acid (FFA). Pathological changes were detected by H&E Staining. Cellular lipid deposition and mitochondrial damage were assessed using Oil Red O, JC-1 staining and transmission electron microscope (TEM), respectively. The intermolecular interaction was identified by dual-luciferase reporter assay, ChIP, and Co-IP. ZNF143 was upregulated in MASLD models, and its knockdown mitigated lipid accumulation and liver injury by activating hepatocyte mitophagy. ZNF143 promoted SMAD-specific E3 ubiquitin-protein ligase 1 (SMURF1) transcription by binding to its promoter region. Moreover, SMURF1 mediated transient receptor potential vanilloid type 1 (TRPV1) ubiquitination and degradation. Finally, knockdown of TRPV1 or overexpression of SMURF1 reversed the promoting effect of ZNF143 knockdown on mitophagy in FFA-treated Huh-7 cells. In short, ZNF143 upregulation exacerbated MASLD progression by mediating TRPV1 ubiquitination and degradation through transcriptionally activating SMURF1. - Source: PubMed
Publication date: 2026/08/11
Long MeiTan KeweiDong Yujie - Endometriosis is a chronic, estrogen-dependent gynecologic disorder characterized by the ectopic growth of endometrial tissue outside the uterus. Zinc finger protein 143 (ZNF143) is a DNA-binding transcription factor, yet its role in endometriosis remains unknown. Here, it is reported that ZNF143 is significantly up-regulated in ectopic endometrial lesions. Invivo, PgrZfp143 mice were used to achieve conditional deletion of Zfp143 in uterine epithelial and stromal cells via progesterone receptor (Pgr)-driven Cre recombination. Uterine-specific deletion of Zfp143 in this model markedly reduced lesion formation and growth. In contrast, epithelial-specific deletion using Sprr2fZfp143 mice, in which Sprr2f is selectively expressed in uterine epithelial cells, showed no significant effect, indicating that ZNF143 primarily functions in endometrial stromal cells. In vitro, ZNF143 promoted stromal cell migration and invasion while knockdown of ZNF143 using siRNA transfection inhibited migration and invasion of hTERT-immortalized human endometrial stromal cells and primary human endometrial stromal cells. ZNF143 deficiency also reduced collagen deposition in ectopic lesions, implicating it in fibrotic remodeling. Transcriptomic profiling identified plasminogen activator inhibitor-1 (SERPINE1) as a key downstream effector mediating ZNF143-driven fibrosis, and SERPINE1 silencing attenuated these profibrotic effects. Collectively, these findings establish ZNF143 as a critical transcriptional regulator, especially in endometrial stroma that drives lesion progression and fibrosis in endometriosis, providing new mechanistic insights and highlighting a promising therapeutic target. - Source: PubMed
Publication date: 2026/06/18
Zhang KekeLi GuojingLi ChendiOuyang JingLuo LiujingYao YutongZhu ChenfengZhang PingLiang YanLin YuXu Hong - Viruses frequently hijack host metabolic enzymes to fuel replication. However, the mechanisms underlying this hijacking and utilization of metabolic enzymes remain poorly understood. In this study, we report a sophisticated mechanism by which porcine reproductive and respiratory syndrome virus (PRRSV) exploits a non-canonical enzymatic function of PHGDH (phosphoglycerate dehydrogenase) to modulate macroautophagy/autophagy. We demonstrate that PRRSV infection recruits the transcription factor ZNF143 (zinc finger protein 143) to transcriptionally repress PHGDH expression. Importantly, the antiviral restriction activity of PHGDH is entirely uncoupled from its canonical enzymatic role in serine biosynthesis. Mechanistically, PHGDH depletion triggers the initiation of autophagy via the AMP-activated protein kinase (AMPK)-ULK1 (unc-51 like autophagy activating kinase 1) signaling axis; however, it paradoxically arrests autophagic flux at the autophagosome-lysosome fusion stage. PHGDH is identified as a critical scaffold that facilitates the assembly of the autophagic soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex; its downregulation disrupts the interaction between STX17 (syntaxin 17) and SNAP29 (synaptosome associated protein 29), thereby blocking autophagosome-lysosome fusion. This induction of incomplete autophagy creates a favorable cytosolic niche for viral replication. Furthermore, the antiviral effect of PHGDH is also observed in two other swine pathogens, porcine epidemic diarrhea virus (PEDV) and pseudorabies virus (PRV). Collectively, these findings revealed that viruses weaponized the moonlighting function of a metabolic enzyme to dismantle autophagic flux, highlighting PHGDH as a broad-spectrum antiviral target that bridged metabolism and membrane trafficking. AMPK: AMP-activated protein kinase; BECN1: beclin 1; CQ: chloroquine; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; MOI: multiplicity of infection; PEDV: porcine epidemic diarrhea virus; PHGDH: phosphoglycerate dehydrogenase; PRV: pseudorabies virus; PRRSV: porcine reproductive and respiratory syndrome virus; SGOC: serine-glycine-one-carbon; siRNA: small interfering RNA; SNAP29: synaptosome associated protein 29; SNARE: soluble N-ethylmaleimide-sensitive factor attachment protein receptor; SQSTM1/p62: sequestosome 1; SSP: serine synthesis pathway; STX17: syntaxin 17; ULK1: unc-51 like autophagy activating kinase 1; VAMP8: vesicle associated membrane protein 8; ZNF143: zinc finger protein 143. - Source: PubMed
Publication date: 2026/06/16
Yu ZhangpingZhou QiongqiongGao PengZhang YongningGe XinnaHan JunGuo XinZhou LeiYang Hanchun - Rhabdomyosarcoma with alveolar morphology is a diagnostically challenging tumor pattern, particularly in cases lacking canonical FOXO1-associated fusions. In the current WHO framework, molecular fusion status plays a central role in classification and risk stratification. However, a subset of tumors lacks canonical rearrangements and harbors alternative genetic events. We report a case of a 4-year-old girl with a massive parameningeal rhabdomyosarcoma presenting with cranial nerve dysfunction and airway compromise. Histological examination confirmed rhabdomyosarcoma with alveolar morphology. Fluorescence in situ hybridization revealed no rearrangements of FOXO1 or PAX3. Targeted RNA sequencing identified a novel NCOA1::ZNF143 fusion transcript. Despite intensive multimodal treatment including chemotherapy, radiotherapy, surgery, and metronomic therapy, the disease demonstrated multiple relapses with subsequent metastatic progression involving the spinal cord and central nervous system, ultimately leading to a fatal outcome. - Source: PubMed
Sharlai Anastasia SStradomskaya Tatyana SKachanov Denis YDruy Alexander EPanferova Agnesa VAbasov RuslanGrachev Nikolai SKonovalov Dmitry M