Ask about this productRelated genes to: DULLARD antibody
- Gene:
- CTDNEP1 NIH gene
- Name:
- CTD nuclear envelope phosphatase 1
- Previous symbol:
- DULLARD
- Synonyms:
- HSA011916, NET56
- Chromosome:
- 17p13.1
- Locus Type:
- gene with protein product
- Date approved:
- 2003-05-22
- Date modifiied:
- 2016-10-05
Related products to: DULLARD antibody
Related articles to: DULLARD antibody
- In open mitosis, a single nuclear envelope (NE) forms around segregated chromosomes despite an excess of membrane-chromatin tethers. Here, we identify a hierarchical relationship between the BAF binding membrane tethers LEM-2 and Emerin, in which LEM-2 preferentially accumulates at BAF binding sites during postmitotic NE assembly and limits Emerin accumulation in embryos. When LEM-2 is absent, Emerin occupies these sites and compensates for LEM-2 loss; however, NE formation becomes sensitized to ER membrane abundance - excessive phospholipid production through loss of CTDNEP1/CNEP-1 causes membrane invasions in interchromosomal regions and, across multiple systems, formation of lobulated, unstable nuclei with abnormal Emerin accumulations. We find that human CTDNEP1 regulates the NE-associated enzyme CCTα to maintain phosphatidylcholine (PC) homeostasis through preventing delayed PC breakdown. Restoring PC levels rescues Emerin assembly and nuclear morphology defects resulting from the combined loss of CTDNEP1 and LEMD2. Together, these findings link membrane-chromatin tethering to ER lipid content and reveal preferential tethering as a determinant of NE assembly fidelity, with broad relevance to disease-related nuclear defects. - Source: PubMed
Publication date: 2026/03/02
Barger Sarah RSepúlveda SofiaYang HanGoudge MarcLee ShokenRidgway Neale DBahmanyar Shirin - Pancreatic ductal adenocarcinoma (PDAC) remains a highly lethal malignancy due to limited therapeutic options. Identifying novel genes that influence its progression is critical. This study aimed to investigate the role of , a phosphatase-encoding gene, in PDAC using multi-omics data from The Cancer Genome Atlas (TCGA). - Source: PubMed
Nii MayukaHayata Tadayoshi - Cytokines of the TGF-β superfamily control essential cell fate decisions via receptor regulated SMAD (R-SMAD) transcription factors. Ligand-induced R-SMAD phosphorylation in the cytosol triggers their activation and nuclear accumulation. We determine how R-SMADs are inactivated by dephosphorylation in the cell nucleus to counteract signaling by TGF-β superfamily ligands. We show that R-SMAD dephosphorylation is mediated by an inner nuclear membrane associated complex containing the scaffold protein MAN1 and the CTDNEP1-NEP1R1 phosphatase. Structural prediction, domain mapping and mutagenesis reveals that MAN1 binds independently to the CTDNEP1-NEP1R1 phosphatase and R-SMADs to promote their inactivation by dephosphorylation. Disruption of this complex causes nuclear accumulation of R-SMADs and aberrant signaling, even in the absence of TGF-β ligands. These findings establish CTDNEP1-NEP1R1 as the R-SMAD phosphatase, reveal the mechanistic basis for TGF-β signaling inactivation and highlight how this process is disrupted by disease-associated MAN1 mutations. - Source: PubMed
Publication date: 2025/04/11
Ji ZheSiu Wing-Yan SkylaDueñas Maria EmiliaMüller LeonieTrost MatthiasCarvalho Pedro - An understanding of the molecular mechanism whereby an environmental chemical causes a disease is important for the purposes of future applications. In this study, a multiomics workflow was designed to combine several publicly available datasets in order to identify CpG sites and genes that mediate the impact of exposure to environmental chemicals on cardiometabolic traits. Organophosphate and prenatal lead exposure were previously reported to change methylation level at the cg23627948 site. The outcome of the analyses conducted in this study revealed that, as the cg23627948 site becomes methylated, the expression of the gene decreases, which leads to a higher body fat percentage. Prenatal perfluorooctane sulfonate exposure was reported to increase the methylation level at the cg21153102 site. Findings of this study revealed that higher methylation at this site contributes to higher diastolic blood pressure by changing the expression of and genes. Moreover, mediates the impact of B12 supplementation → cg05280698 hypermethylation on higher kidney function, while mediates the impact of air pollution → cg03186999 hypomethylation on higher systolic blood pressure. This study investigates CpG sites and genes that mediate the impact of environmental chemicals on cardiometabolic traits. Furthermore, the multiomics approach described in this study provides a convenient workflow with which to investigate the impact of an environmental factor on the body's biomarkers, and, consequently, on health conditions, using publicly available data. - Source: PubMed
Publication date: 2024/07/29
Nikpay Majid - H3.1 histone is predominantly synthesized and enters the nucleus during the G1/S phase of the cell cycle, as a new component of duplicating nucleosomes. Here, we found that p53 is necessary to secure the normal behavior and modification of H3.1 in the nucleus during the G1/S phase, in which p53 increases C-terminal domain nuclear envelope phosphatase 1 (CTDNEP1) levels and decreases enhancer of zeste homolog 2 (EZH2) levels in the H3.1 interactome. In the absence of p53, H3.1 molecules tended to be tethered at or near the nuclear envelope (NE), where they were predominantly trimethylated at lysine 27 (H3K27me3) by EZH2, without forming nucleosomes. This accumulation was likely caused by the high affinity of H3.1 toward phosphatidic acid (PA). p53 reduced nuclear PA levels by increasing levels of CTDNEP1, which activates lipin to convert PA into diacylglycerol. We moreover found that the cytosolic H3 chaperone HSC70 attenuates the H3.1-PA interaction, and our molecular imaging analyses suggested that H3.1 may be anchored around the NE after their nuclear entry. Our results expand our knowledge of p53 function in regulation of the nuclear behavior of H3.1 during the G1/S phase, in which p53 may primarily target nuclear PA and EZH2. - Source: PubMed
Publication date: 2024/06/21
Oikawa TsukasaHasegawa JunyaHanda HarukaOhnishi NaomiOnodera YasuhitoHashimoto AriSasaki JunkoSasaki TakehikoUeda KojiSabe Hisataka