PRMT2 links histone H3R8 asymmetric dimethylation to oncogenic activation and tumorigenesis of glioblastoma
The role of protein arginine methyltransferases (PRMTs) in epigenetic regulation in cancer is still poorly understood. Here, the authors show that PRMT2 is highly expressed in Glioblastoma multiforme (GBM) and provide evidence that PRMT2 acts as a transcriptional co-activator for oncogenic gene expr...
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Nature Portfolio
2018-10-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-018-06968-7 |
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author | Feng Dong Qian Li Chao Yang Dawei Huo Xing Wang Chunbo Ai Yu Kong Xiaoyu Sun Wen Wang Yan Zhou Xing Liu Wei Li Weiwei Gao Wen Liu Chunsheng Kang Xudong Wu |
author_facet | Feng Dong Qian Li Chao Yang Dawei Huo Xing Wang Chunbo Ai Yu Kong Xiaoyu Sun Wen Wang Yan Zhou Xing Liu Wei Li Weiwei Gao Wen Liu Chunsheng Kang Xudong Wu |
author_sort | Feng Dong |
collection | DOAJ |
description | The role of protein arginine methyltransferases (PRMTs) in epigenetic regulation in cancer is still poorly understood. Here, the authors show that PRMT2 is highly expressed in Glioblastoma multiforme (GBM) and provide evidence that PRMT2 acts as a transcriptional co-activator for oncogenic gene expression programs, at least partly dependent on its H3R8me2a activity, in GBM pathogenesis. |
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format | Article |
id | doaj.art-8f79abb72a05486c8ed09b9953768969 |
institution | Directory Open Access Journal |
issn | 2041-1723 |
language | English |
last_indexed | 2024-12-20T20:06:54Z |
publishDate | 2018-10-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Nature Communications |
spelling | doaj.art-8f79abb72a05486c8ed09b99537689692022-12-21T19:27:55ZengNature PortfolioNature Communications2041-17232018-10-019111410.1038/s41467-018-06968-7PRMT2 links histone H3R8 asymmetric dimethylation to oncogenic activation and tumorigenesis of glioblastomaFeng Dong0Qian Li1Chao Yang2Dawei Huo3Xing Wang4Chunbo Ai5Yu Kong6Xiaoyu Sun7Wen Wang8Yan Zhou9Xing Liu10Wei Li11Weiwei Gao12Wen Liu13Chunsheng Kang14Xudong Wu15Department of Cell Biology, Tianjin Medical University, 2011 Collaborative Innovation Center of Tianjin for Medical Epigenetics, Tianjin Key Laboratory of Medical EpigeneticsDepartment of Cell Biology, Tianjin Medical University, 2011 Collaborative Innovation Center of Tianjin for Medical Epigenetics, Tianjin Key Laboratory of Medical EpigeneticsDepartment of Neurosurgery, Tianjin Medical University General HospitalDepartment of Cell Biology, Tianjin Medical University, 2011 Collaborative Innovation Center of Tianjin for Medical Epigenetics, Tianjin Key Laboratory of Medical EpigeneticsDepartment of Cell Biology, Tianjin Medical University, 2011 Collaborative Innovation Center of Tianjin for Medical Epigenetics, Tianjin Key Laboratory of Medical EpigeneticsDepartment of Cell Biology, Tianjin Medical University, 2011 Collaborative Innovation Center of Tianjin for Medical Epigenetics, Tianjin Key Laboratory of Medical EpigeneticsDepartment of Cell Biology, Tianjin Medical University, 2011 Collaborative Innovation Center of Tianjin for Medical Epigenetics, Tianjin Key Laboratory of Medical EpigeneticsDepartment of Cell Biology, Tianjin Medical University, 2011 Collaborative Innovation Center of Tianjin for Medical Epigenetics, Tianjin Key Laboratory of Medical EpigeneticsHubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan UniversityHubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan UniversityDepartment of Neuropathology, Beijing Neurosurgical Institute, Capital Medical University, 6 Tiantanxi LiDepartment of Pathology, Tianjin Nankai HospitalSchool of Pharmaceutical Sciences, Xiamen University, XiamenSchool of Pharmaceutical Sciences, Xiamen University, XiamenDepartment of Neurosurgery, Tianjin Medical University General HospitalDepartment of Cell Biology, Tianjin Medical University, 2011 Collaborative Innovation Center of Tianjin for Medical Epigenetics, Tianjin Key Laboratory of Medical EpigeneticsThe role of protein arginine methyltransferases (PRMTs) in epigenetic regulation in cancer is still poorly understood. Here, the authors show that PRMT2 is highly expressed in Glioblastoma multiforme (GBM) and provide evidence that PRMT2 acts as a transcriptional co-activator for oncogenic gene expression programs, at least partly dependent on its H3R8me2a activity, in GBM pathogenesis.https://doi.org/10.1038/s41467-018-06968-7 |
spellingShingle | Feng Dong Qian Li Chao Yang Dawei Huo Xing Wang Chunbo Ai Yu Kong Xiaoyu Sun Wen Wang Yan Zhou Xing Liu Wei Li Weiwei Gao Wen Liu Chunsheng Kang Xudong Wu PRMT2 links histone H3R8 asymmetric dimethylation to oncogenic activation and tumorigenesis of glioblastoma Nature Communications |
title | PRMT2 links histone H3R8 asymmetric dimethylation to oncogenic activation and tumorigenesis of glioblastoma |
title_full | PRMT2 links histone H3R8 asymmetric dimethylation to oncogenic activation and tumorigenesis of glioblastoma |
title_fullStr | PRMT2 links histone H3R8 asymmetric dimethylation to oncogenic activation and tumorigenesis of glioblastoma |
title_full_unstemmed | PRMT2 links histone H3R8 asymmetric dimethylation to oncogenic activation and tumorigenesis of glioblastoma |
title_short | PRMT2 links histone H3R8 asymmetric dimethylation to oncogenic activation and tumorigenesis of glioblastoma |
title_sort | prmt2 links histone h3r8 asymmetric dimethylation to oncogenic activation and tumorigenesis of glioblastoma |
url | https://doi.org/10.1038/s41467-018-06968-7 |
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