ArticleCancer & metabolism2018
Protein interaction and functional data indicate MTHFD2 involvement in RNA processing and translation.
Article in Cancer & metabolism, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 47 citations in OpenAlex.
- miR-1251-5p inhibits tumorigenesis and metastasis in renal cell carcinoma by targeting MTHFD2.Translational andrology and urology · 2026Article
- MTHFD2: a promising metabolic checkpoint for diseases.Journal of translational medicine · 2026Review
- Integrative analysis of transcriptome and single-cell sequencing combined with experimental validation identifies biomarkers associated with T cell and senescence in sepsis.Scientific reports · 2026Article
- One-carbon metabolism in cancer: moonlighting functions of metabolic enzymes and anti-tumor therapy.Cancer metastasis reviews · 2025Review
- MTHFD2: A Retrospective and a Glance into the Future.International journal of molecular sciences · 2025Review
- Article
- Nuclear localization of MTHFD2 is required for correct mitosis progression.Nature communications · 2024Article
- Selectivity analysis of diaminopyrimidine-based inhibitors of MTHFD1, MTHFD2 and MTHFD2L.Scientific reports · 2024Article
- The one-carbon metabolic enzyme MTHFD2 promotes resection and homologous recombination after ionizing radiation.Molecular oncology · 2024Article
- MTHFD2 in healthy and cancer cells: Canonical and non-canonical functions.npj metabolic health and disease · 2024Review
- Targeting Metabolic Vulnerabilities in Epstein-Barr Virus-Driven Proliferative Diseases.Cancers · 2023Review
- SNHG3/hsa-miR-455-5p Axis-mediated High Expression of MTHFD2 Correlates with Tumor Immune Infiltration and Endometrial Carcinoma Progression.International journal of medical sciences · 2023Article
- Targeting mitochondrial one-carbon enzyme MTHFD2 together with pemetrexed confers therapeutic advantages in lung adenocarcinoma.Cell death discovery · 2022Article
- The catalytic mechanism of the mitochondrial methylenetetrahydrofolate dehydrogenase/cyclohydrolase (MTHFD2).PLoS computational biology · 2022Article
- The Epithelial-Mesenchymal Transition at the Crossroads between Metabolism and Tumor Progression.International journal of molecular sciences · 2022Review
- ATF4/MYC Regulates MTHFD2 to Promote NSCLC Progression by Mediating Redox Homeostasis.Disease markers · 2022Article
- MTHFD2 promotes tumorigenesis and metastasis in lung adenocarcinoma by regulating AKT/GSK-3β/β-catenin signalling.Journal of cellular and molecular medicine · 2021Article
- A Review of Small-Molecule Inhibitors of One-Carbon Enzymes: SHMT2 and MTHFD2 in the Spotlight.ACS pharmacology & translational science · 2021Review
- Therapeutic targeting of the mitochondrial one-carbon pathway: perspectives, pitfalls, and potential.Oncogene · 2021Review
- The TIM22 complex mediates the import of sideroflexins and is required for efficient mitochondrial one-carbon metabolism.Molecular biology of the cell · 2021Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe folate-coupled metabolic enzyme MTHFD2 is overexpressed in many tumor types and required for cancer cell proliferation, and is therefore of interest as a potential cancer therapeutic target. However, recent evidence suggests that MTHFD2 has a non-enzymatic function which may underlie the dependence of cancer cells on this protein. Understanding this non-enzymatic function is important for optimal targeting of MTHFD2 in cancer.
methodsTo identify potential non-enzymatic functions of MTHFD2, we defined its interacting proteins using co-immunoprecipitation and mass spectrometry and integrated this information with large-scale co-expression analysis, protein dynamics, and gene expression response to MTHFD2 knockdown.
resultsWe found that MTHFD2 physically interacts with a set of nuclear proteins involved in RNA metabolism and translation, including components of the small ribosomal subunit and multiple members of the RNA-processing hnRNP family. Interacting proteins were also in general co-expressed with MTHFD2 in experiments that stimulate or repress proliferation, suggesting a close functional relationship. Also, unlike other folate one-carbon enzymes, the MTHFD2 protein has a short half-life and responds rapidly to serum. Finally, shRNA against MTHFD2 depletes several of its interactors and yields an overall transcriptional response similar to targeted inhibition of certain ribosomal subunits.
conclusionsTaken together, our findings suggest a novel function of MTHFD2 in RNA metabolism and translation.
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