ENO1 suppresses cancer cell ferroptosis by degrading the mRNA of iron regulatory protein 1
Ontology highlight
ABSTRACT:
ORGANISM(S): Homo sapiens
PROVIDER: GSE153989 | GEO | 2021/09/10
REPOSITORIES: GEO
Similar Datasets
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: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: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: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: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:Mathematical Definition
symbol/abbreviation
Mathematical symbols
Keq Equilibrium constant
Ki Inhibition constant
Km Affinity constant
v Predicted enzyme activities
Vf Maximal enzyme activities under saturating substrate and activator
conditions, and in the absence of inhibitors
h Hill coefficient
k Rate constant
Abbreviations
ACET Acetaldehyde
ADH Alcohol dehydrogenase
AK Adenylate kinase
ATPcons ATP consuming reactions
bPG 1,3-bisphosphoglycerate
ENO Enolase
ETOHcy Cytoplasmic ethanol
ETOHex Extracellular ethanol
ETOHexp Ethanol transport
GAP Glyceraldehyde 3-phosphate
GAPD Glyceraldehyde 3-phosphate dehydrogenase
GF Glucose facilitator
GK Glucokinase
GLUCcy Cytoplasmic glucose
GLUCex Extracellular glucose
GLUC6P Glucose 6-phosphate
GPD Glucose 6-phosphate dehydrogenase
KDPG 2-keto-3-deoxy-6-phosphogluconate
KDPGA 2-keto-3-deoxy-6-phosphogluconate aldolase
PDC Pyruvate decarboxylase
PEP Phosphoenolpyruvate
PGD 6-phosphogluconate dehydratase
PGK 3-phosphoglycerate kinase
PGL 6-phosphogluconolactonase
PGLACTON 6-phosphogluconolactone
PGLUCONATE 6-phosphogluconate
PGM Phosphoglycerate mutase
P3G 3-phosphoglycerate
P2G 2-phosphoglycerate
PYK Pyruvate kinase
PYR Pyruvate
2020-08-06 | MODEL2008060001 | BioModels
Project description:eCLIP was performed for ENO1 in HeLa cells, following the protocol described by Van Nostrand et al. (2016). Libraries for six immunoprecipitation and size-matched input controls were produced. In addition, libraries were produced for two no-crosslinking controls. The libraries were sequenced using paired-end sequencing (PE125) on an Illumina HiSeq2000 platform.
2020-10-27 | E-MTAB-9031 | biostudies-arrayexpress
Project description:The RNA degradosome is a multi-enzyme assembly that plays a central role in the RNA metabolism of Escherichia coli and numerous other bacterial species including pathogens. The core of the assembly is provided by the endoribonuclease RNase E, one of the largest E. coli proteins. The C-terminal half of RNase E is predicted to be predominantly unstructured and is punctuated with conserved short linear motifs that recruit partner proteins, direct RNA interactions, and enable association with the cytoplasmic membrane. We demonstrate that a subassembly of the degradosome - comprising a 248-residue segment of the C-terminal part of RNase E, the DEAD-box helicase RhlB, and the glycolytic enzyme enolase - serves as a flexible recognition centre that can co-recruit small regulatory RNA (sRNA) molecules and the RNA chaperone Hfq into an effector complex. The association of enolase with the degradosome impacts on carbon utilisation pathways under changing metabolic conditions, most likely by facilitating recruitment and the activity of sRNAs. Our results support a model in which the degradosome captures substrates and regulatory RNAs through the recognition core, facilitates pairing to cognate transcripts, and presents the target to the ribonuclease active sites of the greater assembly for cooperative degradation or processing.
2019-06-01 | GSE100022 | GEO
Project description:mRNA decay in E. Coli degradosome mutants and their parental strains following transcriptional arrest with rifampicin. Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes. An RNA stablity experiment design type examines stability and/or decay of RNA transcripts. User Defined
2006-01-05 | E-GEOD-3978 | biostudies-arrayexpress