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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Main Authors: 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
Format: Article
Language:English
Published: Nature Portfolio 2018-10-01
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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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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