Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Nuclear MTHFD2 secures centromere methylation, chromosome stability and correct mitosis progression

ABSTRACT: Nuclear MTHFD2 secures centromere methylation, chromosome stability and correct mitosis progression

PROVIDER: PRJEB61666 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	ERR11274950.fastq.gz	Fastqsanger.gz
	ERR11274951.fastq.gz	Fastqsanger.gz
	ERR11274952.fastq.gz	Fastqsanger.gz
	ERR11274953.fastq.gz	Fastqsanger.gz
	ERR11274954.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 6

Similar Datasets

Nuclear MTHFD2 secures centromere methylation, chromosome stability and correct mitosis progression

Project description:Subcellular compartmentalization of metabolic enzymes may elicit specific cellular functions by establishing a unique metabolic environment. Indeed, the nuclear translocation of certain metabolic enzymes is required for epigenetic regulation and gene expression control. Here, we reveal that, in cancer cells, the mitochondrial enzyme methylenetetrahydrofolate dehydrogenase 2 (MTHFD2) localizes in the nucleus during the G2-M phase of the cell cycle to secure mitosis progression. Nuclear MTHFD2 interacts with proteins involved in mitosis regulation and centromere stability, including the methyltransferases KMT5A and DNMT3B. Loss of MTHFD2 induces centromere overexpression and severe methylation defects, and impedes correct mitosis completion. As a consequence, MTHFD2 deficient cells accumulate chromosomal aberrations arising from chromosome congression and segregation defects. Blocking the catalytic nuclear function of MTHFD2 recapitulates the phenotype observed in MTHFD2 deficient cells, attributing to nuclear MTHFD2 an enzymatic active role in controlling mitosis. Our discovery uncovers a nuclear moonlighting role for the cancer target MTHFD2, and emphasizes that cancer metabolism rewiring may encompass the relocation of metabolic enzymes to alternative subcellular compartments.

2024-07-26 | GSE232307 | GEO

Nuclear MTHFD2 secures centromere methylation, chromosome stability and correct mitosis progression

Project description:Nuclear MTHFD2 secures centromere methylation, chromosome stability and correct mitosis progression

| PRJNA971587 | ENA

Nuclear MTHFD2 secures centromere methylation, chromosome stability and correct mitosis progression

2024-11-28 | PXD041821 | Pride

Nuclear MTHFD2 secures centromere methylation, chromosome stability and correct mitosis progression [RNA-seq]

2024-07-26 | GSE230750 | GEO

Nuclear MTHFD2 secures centromere methylation, chromosome stability and correct mitosis progression [RNA-seq]

Project description:Nuclear MTHFD2 secures centromere methylation, chromosome stability and correct mitosis progression [RNA-seq]

| PRJNA962510 | ENA

Centromere Pairing Enables Correct Segregation of Meiotic Chromosomes

Project description:Centromere Pairing Enables Correct Segregation of Meiotic Chromosomes

| PRJNA1069033 | ENA

Nuclear localization of MTHFD2 is required for correct mitosis progression.

Project description:Subcellular compartmentalization of metabolic enzymes establishes a unique metabolic environment that elicits specific cellular functions. Indeed, the nuclear translocation of certain metabolic enzymes is required for epigenetic regulation and gene expression control. Here, we show that the nuclear localization of the mitochondrial enzyme methylenetetrahydrofolate dehydrogenase 2 (MTHFD2) ensures mitosis progression. Nuclear MTHFD2 interacts with proteins involved in mitosis regulation and centromere stability, including the methyltransferases KMT5A and DNMT3B. Loss of MTHFD2 induces severe methylation defects and impedes correct mitosis completion. MTHFD2 deficient cells display chromosome congression and segregation defects and accumulate chromosomal aberrations. Blocking the catalytic nuclear function of MTHFD2 recapitulates the phenotype observed in MTHFD2 deficient cells, whereas restricting MTHFD2 to the nucleus is sufficient to ensure correct mitotic progression. Our discovery uncovers a nuclear role for MTHFD2, supporting the notion that translocation of metabolic enzymes to the nucleus is required to meet precise chromatin needs.

| S-EPMC11557897 | biostudies-literature

Knock down of MTHFD2 of lung adenocarcinoma cell line H322

Project description:Lung cancer is leading cause of cancer-related death in the world, because of high recurrence rate and acquired resistance to targeting drugs such as gefitinib. Here we uncover a critical MTHFD2 enzyme-mediated purine synthesis pathway in mitochondria in poor prognostic lung cancer. Expression of MTHFD2 was induced by epidermal growth factor (EGF) stimulation. It was overexpressed in gefitinib-resistant cancer cells and high-grade tumor tissues. Knockdown of MTHFD2 significantly decreased not only in vitro and in vivo cell growth but also tumor sphere formation and tumor initiating activity, properties of cancer stem-like cells. Integrated analysis of metabolome and transcriptome of MTHFD2 knocked-down cells revealed significant accumulation of the nucleotide intermediates before MTHFD2-mediated one carbon transfer and marked deficiency of purine nucleotides required for cell growth. Thus we provide evidence that MTHFD2 pathway is critical for growth of both cancer cells and cancer stem-like cells as an Achilles heel to eradicate tumors in poor prognostic lung cancer.

2019-07-02 | GSE84007 | GEO

MTHFD2-mediated ubiquitination and degradation of FOXO1 promote tongue squamous cell carcinoma progression

Project description:In recent years, there has been an increasing focus on Methylenetetrahydrofolate Dehydrogenase 2 (MTHFD2), a key enzyme in one-carbon metabolism, and its expression levels and mechanisms in tumors. Research has shown that MTHFD2 is upregulated in various malignant tumors and is closely associated with tumor onset, progression, and prognosis. However, the role and mechanisms of MTHFD2 in Tongue Squamous Cell Carcinoma (TSCC) remain unclear. Our study found that MTHFD2 expression is significantly elevated in TSCC and is closely linked to poor prognosis. Furthermore, the knockdown of MTHFD2 notably impacts the proliferation and migration capabilities of TSCC cells. Therefore, MTHFD2 holds promise as a crucial therapeutic target for TSCC.

2025-11-06 | GSE275423 | GEO

BMPR1A-mediated BMP signalling ensures correct mitosis-to-meiosis transition in mouse fetal ovarian germ cells, in vivo

Project description:A successful mitosis-to-meiosis transition in germ cells is essential for fertility in sexually reproducing organisms. In mice and humans, it is established that STRA8 expression is critical for meiotic onset in both sexes. Here we show that BMP signalling is also essential, not for STRA8 induction but for correct meiotic progression in mouse fetal ovarian germ cells. Germ cell-specific deletion of Bmpr1a caused aberrant expression of meiotic, pluripotency, and cell cycle genes in E14.5 mouse fetal ovaries. Our results verify a role for BMP signalling in instructing germ cell meiosis in female mice in vivo, and shed light on the regulatory mechanisms underlying fetal germ cell development.

2025-01-16 | GSE268565 | GEO

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data