ArticleJournal of molecular biology2009
Direct binding of glyceraldehyde 3-phosphate dehydrogenase to telomeric DNA protects telomeres against chemotherapy-induced rapid degradation.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 88 citations in OpenAlex.
- The role and therapeutic potential of glucose metabolism in multidrug resistance of cancer.Frontiers in cell and developmental biology · 2025Review
- Endogenous Cellular Metabolite Methylglyoxal Induces DNA-Protein Cross-Links in Living Cells.ACS chemical biology · 2024Article
- Immunomodulation of Cancer Cells Using Autologous Blood Concentrates as a Patient-Specific Cell Culture System: A Comparative Study on Osteosarcoma and Fibrosarcoma Cell Lines.Bioengineering (Basel, Switzerland) · 2024Article
- Identification and expression profiling ofFrontiers in plant science · 2024Article
- GAPDH facilitates homologous recombination repair by stabilizing RAD51 in an HDAC1-dependent manner.EMBO reports · 2023Article
- Regulation of tumor metabolism by post translational modifications on metabolic enzymes.Cancer gene therapy · 2023Review
- In silico Identification of Hypoxic Signature followed by reverse transcription-quantitative PCR Validation in Cancer Cell LinesIranian biomedical journal · 2023Article
- Many Functions of Telomerase Components: Certainties, Doubts, and Inconsistencies.International journal of molecular sciences · 2022Review
- Sperm-Specific Glycolysis Enzyme Glyceraldehyde-3-Phosphate Dehydrogenase Regulated by Transcription Factor SOX10 to Promote Uveal Melanoma Tumorigenesis.Frontiers in cell and developmental biology · 2021Article
- Lactate Dehydrogenase-A (LDH-A) Preserves Cancer Stemness and Recruitment of Tumor-Associated Macrophages to Promote Breast Cancer Progression.Frontiers in oncology · 2021Article
- Glyceraldehyde-3-Phosphate Dehydrogenase Increases the Adhesion ofInternational journal of molecular sciences · 2020Article
- The Writers, Readers, and Erasers in Redox Regulation of GAPDH.Antioxidants (Basel, Switzerland) · 2020Review
- Investigating the Role of Telomere and Telomerase Associated Genes and Proteins in Endometrial Cancer.Methods and protocols · 2020Article
- Glyceraldehyde-3-phosphate Dehydrogenase is a Multifaceted Therapeutic Target.Pharmaceutics · 2020Review
- Identification of driver genes associated with chemotherapy resistance of Ewing's sarcoma.OncoTargets and therapy · 2018Article
- Retrospective Proteomic Screening of 100 Breast Cancer Tissues.Proteomes · 2017Article
- RNA-binding proteins related to stress response and differentiation in protozoa.World journal of biological chemistry · 2016Review
- Moonlighting proteins in cancer.Cancer letters · 2016Review
- Protein Recognition in Drug-Induced DNA Alkylation: When the Moonlight Protein GAPDH Meets S23906-1/DNA Minor Groove Adducts.International journal of molecular sciences · 2015Review
- How do glycolytic enzymes favour cancer cell proliferation by nonmetabolic functions?Oncogene · 2015Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is a glycolytic enzyme that displays several non-glycolytic activities, including the maintenance and/or protection of telomeres. In this study, we determined the molecular mechanism and biological role of the interaction between GAPDH and human telomeric DNA. Using gel-shift assays, we show that recombinant GAPDH binds directly with high affinity (K(d)=45 nM) to a single-stranded oligonucleotide comprising three telomeric DNA repeats, and that nucleotides T1, G5, and G6 of the TTAGGG repeat are essential for binding. The stoichiometry of the interaction is 2:1 (DNA:GAPDH), and GAPDH appears to form a high-molecular-weight complex when bound to the oligonucleotide. Mutation of Asp32 and Cys149, which are localized to the NAD-binding site and the active-site center of GAPDH, respectively, produced mutants that almost completely lost their telomere-binding functions both in vitro and in situ (in A549 human lung cancer cells). Treatment of A549 cells with the chemotherapeutic agents gemcitabine and doxorubicin resulted in increased nuclear localization of expressed wild-type GAPDH, where it protected telomeres against rapid degradation, concomitant with increased resistance to the growth-inhibitory effects of these drugs. The non-DNA-binding mutants of GAPDH also localized to the nucleus when expressed in A549 cells, but did not confer any significant protection of telomeres against chemotherapy-induced degradation or growth inhibition; this occurred without the involvement of caspase activation or apoptosis regulation. Overall, these data demonstrate that GAPDH binds telomeric DNA directly in vitro and may have a biological role in the protection of telomeres against rapid degradation in response to chemotherapeutic agents in A549 human lung cancer cells.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.