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ENO1 influences ATP pool of cytoplasm and lactate homeostasis by regulating glycolysis to promote tumor stemness and metastasis

ABSTRACT: This study demonstrated the role of the glycolytic enzyme alpha-enolase (ENO1) on glycolysis and stemness in gastric cancer (GC). High ENO1 expression was associated with poor prognosis and promoted malignant phenotypes and stem-like characteristics in GC. Mechanistically, ENO1 directly stimulated lactate and ATP production by regulating glycolysis, affecting lactate homeostasis and intracellular ATP pools, and co-regulating the AMPK/mTOR and PI3K/AKT signaling pathways. This ultimately drove GC stemness, epithelial-mesenchymal transition (EMT)-related markers, self-renewal, migration, and invasion.

ORGANISM(S): Homo sapiens

PROVIDER: GSE307717 | GEO | 2025/09/27

REPOSITORIES: GEO

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ENO1 influences ATP pool of cytoplasm and lactate homeostasis by regulating glycolysis to promote tumor stemness and metastasis

Project description:ENO1 influences ATP pool of cytoplasm and lactate homeostasis by regulating glycolysis to promote tumor stemness and metastasis

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ENO1 promotes liver carcinogenesis through YAP1-dependent arachidonic acid metabolism

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.

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PCNA regulates metabolism by stabilizing ENO1 and 6PGD

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2023-03-10 | PXD028314 | Pride

ENO1 suppresses cancer cell ferroptosis by degrading the mRNA of iron regulatory protein 1

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.

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ENO1 couples HDAC1 to regulate histone lactylation and gene transcription

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.

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Exon Skipping of Ste20-Like Kinase Enhances Glycolysis and Tumor Progression by Activating Enolase 1 mediated Phosphoenolpyruvate Production

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.

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ENO1-IT1(ENSG00000236269.1) coordinates the acetylation of histone genome-wide in Colorectal Cancer

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

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CARM1 inhibits ferroptosis in bladder cancer cells by upregulating the expression of ENO1

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.

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ENO1 siRNA knockdown in Human HeLa cells

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

Melatonin inhibited tumorigenesis of bladder cancer via suppressing PPARγ/ENO1 mediated glycolysis

Project description:Bladder cancer (BLCA) is one of the most malignant human cancers in the world. The increasingly prominent phenomenon of chemoresistance has become an essential obstacle to clinical treatment for BLCA, and there is an urgent need to explore novel drugs to improve the current clinical status. Melatonin is a well-known natural hormone that showed a potential anti-cancer effect in multiple human cancers. In our study, we comprehensively explored the inhibitory effect of melatonin on BLCA and found that it could suppress the glycolysis process in BLCA cells. Moreover, we discovered that the ninth step enzyme ENO1 of glycolysis was the downstream effector of melatonin and could be a predictive biomarker of BLCA patients.

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