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
- 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, in which Zfp143 is deleted in both uterine epithelial and stromal cells since progesterone receptor expression in these compartments. 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 - Hypomethylating agents (HMAs) are a mainstay of therapy for myeloid cancers, but genetic biomarkers do not predict who will respond to treatment. Using a variety of single-cell sequencing approaches to define the epigenomic state of responder and nonresponder leukemic cells, we demonstrate that leukemic stem cells (LSC) exist in at least two different epigenomic states: a hematopoietic stem cell (HSC)-or multipotent progenitor (MPP)-like state that is sensitive to HMAs, independent of genetic mutations, or a lymphoid-primed MPP (LMPP)-like nonresponder state. Hypomethylation and chromatin accessibility at ZNF143- and CTCF-binding sites results in activation of HOXB4, which defines the HSC/MPP-like state and HMA-sensitivity. Our study provides evidence that the epigenomic state of the LSC is a major determinant of response to HMAs, and demonstrates that a routine clinical assay can identify patients who will respond. - Source: PubMed
Publication date: 2026/05/22
Gopal AparnaTam DerekMey FranziskaLin DianaMay ChristinaJiang JihongBridgers JoshuaCaswell BrettO'Neill KieranVizeacoumar Frederick SMacAuley MackenzieHaniak EmilieCraddock CharlesVyas PareshMalcovati LucaBuckstein RenaMoksa MichelleHirst MartinVizeacoumar Franco JMedvedev NadiaHeuser MichaelStubbins Ryan JDeng YuKarsan Aly - Hongwu mixture (HWM) consists of Taxus chinensis, Marsdenia tenacissima, Rhizoma Curcumae, and Semen coicis. The objective of this study was to ascertain the potential role of the Hongwu mixture (HWM) in the treatment of triple-negative breast cancer (TNBC). TNBC cells were treated with low, medium, and high doses of HWM, and CCK-8 assays were conducted to evaluate the impact of different doses of HWM on TNBC cell viability. The target molecules of HWM were predicted using RNA-sequencing, and molecular docking models between HWM components and target proteins were developed. As the dose of HWM increased, TNBC cell viability gradually decreased. HWM inhibited the proliferation and mobility of TNBC cells, slowed the tumor growth, and upregulated the apoptosis of TNBC cells. HWM promoted Zinc finger protein 143 (ZNF143)-mediated transcriptional activation of salvador family WW domain-containing protein 1 (SAV1) by stabilizing ZNF143 protein expression, leading to phosphorylation of large tumor suppressor homolog 1 (LATS1) and Yes-associated protein 1 (YAP1). Knockdown of ZNF143/SAV1 signaling impaired the therapeutic effect of HWM, and treatment with verteporfin, pharmacological inhibition of YAP/TAZ, reversed the effects of knockdown of SAV1. Therefore, HWM might offer a potent strategy for managing TNBC effectively. - Source: PubMed
Publication date: 2026/03/27
Wu AipingMa JunWang QiongChen AifeiLv WenlingZhang YuZhang Hongying