Moonlighting functions of phosphoglycerate dehydrogenase in cancer
Summary: Phosphoglycerate dehydrogenase (PHGDH) is traditionally known for catalyzing the conversion of 3-phosphoglycerate (3-PG) to 3-phosphonooxypyruvate (3-PHP), a key step in the de novo synthesis of serine. However, recent studies have uncovered that PHGDH exhibits a wide range of non-canonical...
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| Format: | Article |
| Language: | English |
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Elsevier
2025-07-01
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| Series: | Cell Reports |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2211124725007119 |
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| author | Chuanlong Wang Sanqi An Lingyang Zhao Shuo Li Jia Huang Wenkai Ren |
| author_facet | Chuanlong Wang Sanqi An Lingyang Zhao Shuo Li Jia Huang Wenkai Ren |
| author_sort | Chuanlong Wang |
| collection | DOAJ |
| description | Summary: Phosphoglycerate dehydrogenase (PHGDH) is traditionally known for catalyzing the conversion of 3-phosphoglycerate (3-PG) to 3-phosphonooxypyruvate (3-PHP), a key step in the de novo synthesis of serine. However, recent studies have uncovered that PHGDH exhibits a wide range of non-canonical functions. In addition to its role in metabolic reactions within the glycolytic pathway, PHGDH also participates in the regulation of gene transcription and translation. These newly identified functions significantly alter our understanding of how PHGDH aberrantly regulates tumor cell fate. In this review, we summarize the mechanisms by which PHGDH promotes cancer progression through these non-canonical pathways, potentially offering new therapeutic avenues for cancer. |
| format | Article |
| id | doaj-art-5ac38d8529cd46caa6677ac47f41939b |
| institution | Kabale University |
| issn | 2211-1247 |
| language | English |
| publishDate | 2025-07-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Cell Reports |
| spelling | doaj-art-5ac38d8529cd46caa6677ac47f41939b2025-08-20T03:29:15ZengElsevierCell Reports2211-12472025-07-0144711594010.1016/j.celrep.2025.115940Moonlighting functions of phosphoglycerate dehydrogenase in cancerChuanlong Wang0Sanqi An1Lingyang Zhao2Shuo Li3Jia Huang4Wenkai Ren5The First Affiliated Hospital of Guangxi Medical University, Nanning 530021, China; Guangdong Laboratory of Lingnan Modern Agriculture, State Key Laboratory of Swine and Poultry Breeding Industry, College of Animal Science, South China Agricultural University, Guangzhou 510642, ChinaGuangxi Key Laboratory of AIDS Prevention and Treatment & Guangxi Colleges and Universities Key Laboratory of Prevention and Control of Highly Prevalent Diseases, School of Public Health, Guangxi Medical University, Nanning 530021, ChinaGuangdong Laboratory of Lingnan Modern Agriculture, State Key Laboratory of Swine and Poultry Breeding Industry, College of Animal Science, South China Agricultural University, Guangzhou 510642, ChinaGuangdong Laboratory of Lingnan Modern Agriculture, State Key Laboratory of Swine and Poultry Breeding Industry, College of Animal Science, South China Agricultural University, Guangzhou 510642, ChinaGuangdong Laboratory of Lingnan Modern Agriculture, State Key Laboratory of Swine and Poultry Breeding Industry, College of Animal Science, South China Agricultural University, Guangzhou 510642, ChinaThe First Affiliated Hospital of Guangxi Medical University, Nanning 530021, China; Guangdong Laboratory of Lingnan Modern Agriculture, State Key Laboratory of Swine and Poultry Breeding Industry, College of Animal Science, South China Agricultural University, Guangzhou 510642, China; Corresponding authorSummary: Phosphoglycerate dehydrogenase (PHGDH) is traditionally known for catalyzing the conversion of 3-phosphoglycerate (3-PG) to 3-phosphonooxypyruvate (3-PHP), a key step in the de novo synthesis of serine. However, recent studies have uncovered that PHGDH exhibits a wide range of non-canonical functions. In addition to its role in metabolic reactions within the glycolytic pathway, PHGDH also participates in the regulation of gene transcription and translation. These newly identified functions significantly alter our understanding of how PHGDH aberrantly regulates tumor cell fate. In this review, we summarize the mechanisms by which PHGDH promotes cancer progression through these non-canonical pathways, potentially offering new therapeutic avenues for cancer.http://www.sciencedirect.com/science/article/pii/S2211124725007119CP: CancerCP: Metabolism |
| spellingShingle | Chuanlong Wang Sanqi An Lingyang Zhao Shuo Li Jia Huang Wenkai Ren Moonlighting functions of phosphoglycerate dehydrogenase in cancer Cell Reports CP: Cancer CP: Metabolism |
| title | Moonlighting functions of phosphoglycerate dehydrogenase in cancer |
| title_full | Moonlighting functions of phosphoglycerate dehydrogenase in cancer |
| title_fullStr | Moonlighting functions of phosphoglycerate dehydrogenase in cancer |
| title_full_unstemmed | Moonlighting functions of phosphoglycerate dehydrogenase in cancer |
| title_short | Moonlighting functions of phosphoglycerate dehydrogenase in cancer |
| title_sort | moonlighting functions of phosphoglycerate dehydrogenase in cancer |
| topic | CP: Cancer CP: Metabolism |
| url | http://www.sciencedirect.com/science/article/pii/S2211124725007119 |
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