Ontology highlight
ABSTRACT:
PROVIDER: PRJNA1213289 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR32057818_1.fastq.gz | Fastqsanger.gz | |||
| SRR32057818_2.fastq.gz | Fastqsanger.gz | |||
| SRR32057819_1.fastq.gz | Fastqsanger.gz | |||
| SRR32057819_2.fastq.gz | Fastqsanger.gz |
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Project description:ENO1 (α-Enolase 1) is a key glycolytic enzyme that catalyzes the dehydratation of 2-phosphoglycerate to phosphoenolpyruvate. It also belongs to a member of the RNA degradosome of Escherichia coli and facilitates RNA degradation, but it’s currently unknown whether ENO1 possesses similar function in eukaryotes. To test this possibility,we performed RNA-seq assays expressing NTC or ENO1 shRNA, respectively.
2021-09-10 | GSE153989 | GEO
Project description:Enolase 1 (ENO1) is a glycolytic enzyme that plays essential roles in various pathological activities including cancer development. However, the mechanisms underlying ENO1-contributed tumorigenesis are not well explained. Here, we uncover that ENO1, as an RNA-binding protein, binds to the cytosine-uracil-guanine-rich elements of YAP1 messenger RNA to promote its translation. ENO1 and YAP1 positively regulate alternative arachidonic acid (AA) metabolism by inverse regulation of PLCB1 and HPGD (15-hydroxyprostaglandin dehydrogenase). The YAP1/PLCB1/HPGD axis-mediated activation of AA metabolism and subsequent accumulation of prostaglandin E2 (PGE2) are responsible for ENO1-mediated cancer progression, which can be retarded by aspirin. Finally, aberrant activation of ENO1/YAP1/PLCB1 and decreased HPGD expression in clinical hepatocellular carcinoma samples indicate a potential correlation between ENO1-regulated AA metabolism and cancer development. These findings underline a new function of ENO1 in regulating AA metabolism and tumorigenesis, suggesting a therapeutic potential for aspirin in patients with liver cancer with aberrant expression of ENO1 or YAP1.
2023-05-19 | GSE183703 | GEO
Project description:Histone deacetylases (HDACs) are essential transcriptional regulators that mediate gene expression through the complexes they are involved in. Thus, deciphering the HDAC-associated proteins is key to elucidating the underlying mechanisms. Here we present an efficient tool, termed heterobifunctional molecule-enabled proximity labeling strategy (BimPL), to investigate endogenous HDAC neighboring proteins in living cells. Leveraging BimPL and quantitative proteomics, we enable the robust capture of several known HDAC complexes as well as numerous putative HDAC interactors such as glycolytic enzyme enolase-1 (ENO1). Through biochemical studies and CUT&Tag analysis, we uncovered that nuclear ENO1 interacts with HDAC1, which in turn blunts the activity of HDAC1 via locally generated phosphoenolpyruvate (PEP), thereby mediating histone lysine lactylation (Kla) and gene transcription. Our study offers a versatile tool for systematic exploring endogenous protein complexes, as well as provides insight into the unidentified function of ENO1 in the regulation of histone Kla and liver tumor progression.
2025-05-01 | GSE291520 | GEO
Project description:Dysregulated RNA splicing is activated in tumors; however, the metabolic landscape and consequent implications of this process remain largely unexplored. In this study, we identified exon skipping in Ste20-like kinase (SLK), resulting in a variant isoform of SLK (SLKv), which promotes glycolysis in tumor cells. Mechanistically, SLKv enhances the activity of enolase 1 (ENO1) by binding and phosphorylating the ENO1 serine 2 residue. This modification increases the efficiency of ENO1 in catalyzing the production of phosphoenolpyruvate (PEP). Notably, the accumulation of PEP further accelerates glycolysis by binding to and activating the glycolytic enzyme hexokinase 2 (HK2), phosphofructokinase muscle (PFKM), and phosphoglycerate mutase 1 (PGAM1). Meanwhile, transforming growth factor β (TGFβ) promotes exon skipping of SLK by upregulating the splicing factor KH RNA binding domain containing, signal transduction associated 1 (KHDRBS1). The application of antisense oligonucleotides (ASO) that target SLKv hinders glycolysis and tumorigenesis. These findings establish SLKv as a critical promoter of glycolysis and present a novel metabolic target for cancer therapy.
2025-06-17 | GSE299345 | GEO
Project description:The essential roles of PCNA as a scaffold protein in DNA replication and repair are well established, while its more recently discovered cytosolic roles are less explored. Alpha-enolase (ENO1) and 6-phosphogluconate dehydrogenase (6PGD), important proteins in glycolysis and the Pentose Phosphate Pathway (PPP), respectively, both contain PCNA interacting motifs. Here we show reduced binding to PCNA when the PCNA interacting motif APIM in ENO1 is mutated. Mutant cells have lower ENO1 protein levels, have reduced glucose consumption, altered glycolytic metabolite and nucleoside phosphate pools and increased activation of the citric acid cycle (TCA) compared to parental cells. Treatment of a panel of haematological cell lines with a cell penetrating peptide containing APIM (ATX-101), lead to a metabolic shift with reduction in glycolytic metabolite and nucleoside phosphate pools as well reduced levels of ENO1 and 6PGD proteins. These results suggests that PCNA stabilize ENO1 and 6PGD, and that targeting PCNA reduce the glycolysis, PPP and nucleoside phosphate pools via destabilization of these proteins.
2023-03-10 | PXD028314 | Pride
Project description:Background: Our former study demonstrated that anti-trophoblast antibodies (ATAB) are more prevalent in the sera of patients with unexplained recurrent miscarriages (uRM), and the detection of ATAB is restricted to binding to JEG-3 cells and the quantification by flow cytometry. We further proved that the ATAB-positive sera decrease the production of β-hCG and progesterone in the same cell model. The specific antigenic epitopes of ATAB are still unclear, therefore our aim was to identify one specific target of ATAB in uRM patients. Methods: The possible targets of ATAB were identified by western blots and mass spectrometry, and α-Enolase (ENO1) was further confirmed by a competition assay. The level of anti-ENO1 antibodies in the sera and the production of β-hCG and progesterone were evaluated with enzyme-linked immunosorbent assay (ELISA). Additionally, the expression of ENO1 in the first trimester placenta was analyzed with immunohistochemistry and triple fluorescence staining in uRM patients and healthy controls. Findings: ENO1 was identified to be a prominent target of ATAB and anti-ENO1 antibodies can decrease the secretion of β-hCG and progesterone. The titer of anti-ENO1 antibodies was increased in the sera of ATAB-positive patients compared to ATAB-negative patients. Overexpression of ENO1 and co-expression of ENO1 and β-arrestin was found in the extra villous trophoblasts of uRM patients in the first trimester placenta. Interpretation: Anti-ENO1 antibody in the sera may be a novel autoimmune biomarker of uRM. Decreasing anti-ENO1 antibodies or inhibiting ENO1 expression might be a potential therapeutic treatment for uRM patients.
2019-03-05 | PXD012478 | Pride
Project description:Coactivator-associated arginine methyltransferase 1 (CARM1) is a protein that helps regulate gene expression. Research has shown that CARM1 is also involved in autophagy, RNA regulation, and cancer development, in addition to its primary role in transcriptional regulation. However, its molecular mechanisms and biological consequences in tumor pathogenesis have not been fully elucidated. Our investigation revealed that the overexpression of CARM1 resulted in the upregulation of α-enolase 1 (ENO1), hence enhancing the proliferation, migration, and invasion of bladder cancer (BC) cells. Our findings suggest that the upregulation of ENO1 expression hinders the occurrence of ferroptosis in BC cells by affecting the ACO1/MFRN1 pathway. Through in vivo and in vitro analyses, we discovered that the CARM1-mediated suppression of ferroptosis in BC cells can be partially reversed by using a specific inhibitor: CARM1-IN-3 dihydrochloride (CI3D). This inhibitor also has the ability to inhibit the growth of BC. Collectively, our data indicate that CARM1 could serve as a new oncogenic component in BC and that suppressing CARM1 activity is a promising viable treatment strategy.
2025-03-18 | GSE261843 | GEO
Project description:LncRNA ENO1-IT1 has been found to be mainly located in the nucleus of colorectal mucosa epithelial cells, which indicates that this lncRNA may be responsible for regulating the expression of target gene. To address whether ENO1-IT1 modulates epigenetic changes genome-wide, we performed chromatin immunoprecipitation coupled with high-throughput sequencing (ChIP-seq) in HCT116 cells
2022-10-25 | GSE139403 | GEO
Project description:HeLa cells were either treated with ENO1 or control siRNAs using the protocol of the RNAiMax reagent (ENO1 pool: SMARTpool ON-TARGETplus L-004034-00-0005 and control pool: ON-TARGETplus non-targeting siRNAs 1-4). Three replicates per condition were produced.
2020-10-27 | E-MTAB-9032 | biostudies-arrayexpress
Project description:We systematically evaluated the expression pattern and function of ENO1 in AML. Knockdown ENO1 significantly inhibited ERK pathway phosphorylation, ERK pathway inhibitors significantly inhibited proliferation, clonal formation, migration and invasion of AML cells in vitro, blocked cell cycle and promoted apoptosis of AML cells, and activators of ERK pathway could reverse the effects of knockdown ENO1 on AML cells. The results showed that knockdown ENO1 inhibited the proliferation and invasion of AML cells in mice by inhibiting the activation of ERK pathway, and induced a significant increase in the overall survival rate of mice. Overall, this study aims to explore the role of ENO1 in the development and progression of AML and its potential mechanism, in order to provide a potential target for the treatment of AML.
2024-07-30 | GSE272844 | GEO