NatD promotes lung cancer progression by preventing histone H4 serine phosphorylation to activate Slug expression

NatD is an acetyltransferase responsible for N-α-terminal acetylation of the histone H4 and H2A and has been linked to cell growth. Here the authors show that NatD-mediated acetylation of histone H4 serine 1 competes with the phosphorylation by CK2α at the same residue thus leading to the upregulati...

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Main Authors:	Junyi Ju, Aiping Chen, Yexuan Deng, Ming Liu, Ying Wang, Yadong Wang, Min Nie, Chao Wang, Hong Ding, Bing Yao, Tao Gui, Xinyu Li, Zhen Xu, Chi Ma, Yong Song, Marc Kvansakul, Ke Zen, Chen-Yu Zhang, Cheng Luo, Ming Fang, David C. S. Huang, C. David Allis, Renxiang Tan, Changjiang Kathy Zeng, Jiwu Wei, Quan Zhao
Format:	Article
Language:	English
Published:	Nature Publishing Group 2017-10-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/s41467-017-00988-5

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spelling	doaj-6a59395fcee24917b56f36386d89135b2021-05-11T07:40:03ZengNature Publishing GroupNature Communications2041-17232017-10-018111410.1038/s41467-017-00988-5NatD promotes lung cancer progression by preventing histone H4 serine phosphorylation to activate Slug expressionJunyi Ju0Aiping Chen1Yexuan Deng2Ming Liu3Ying Wang4Yadong Wang5Min Nie6Chao Wang7Hong Ding8Bing Yao9Tao Gui10Xinyu Li11Zhen Xu12Chi Ma13Yong Song14Marc Kvansakul15Ke Zen16Chen-Yu Zhang17Cheng Luo18Ming Fang19David C. S. Huang20C. David Allis21Renxiang Tan22Changjiang Kathy Zeng23Jiwu Wei24Quan Zhao25The State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing UniversityJiangsu Key Laboratory of Molecular Medicine, Medical School, Nanjing UniversityThe State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing UniversityThe State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing UniversityThe State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing UniversityThe State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing UniversityThe State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing UniversityInstitute of Life Sciences, Southeast UniversityDrug Discovery and Design Center, State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of SciencesThe State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing UniversityThe State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing UniversityThe State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing UniversityDepartment of Medical Biology, The Walter and Eliza Hall Institute of Medical Research, University of MelbourneThe State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing UniversityJiangsu Key Laboratory of Molecular Medicine, Medical School, Nanjing UniversityDepartment of Biochemistry, La Trobe UniversityThe State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing UniversityThe State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing UniversityDrug Discovery and Design Center, State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of SciencesInstitute of Life Sciences, Southeast UniversityDepartment of Medical Biology, The Walter and Eliza Hall Institute of Medical Research, University of MelbourneLaboratory of Chromatin Biology and Epigenetics, The Rockefeller UniversityThe State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing UniversitySQJ Biotechnologies LimitedJiangsu Key Laboratory of Molecular Medicine, Medical School, Nanjing UniversityThe State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Nanjing UniversityNatD is an acetyltransferase responsible for N-α-terminal acetylation of the histone H4 and H2A and has been linked to cell growth. Here the authors show that NatD-mediated acetylation of histone H4 serine 1 competes with the phosphorylation by CK2α at the same residue thus leading to the upregulation of Slug and tumor progression.https://doi.org/10.1038/s41467-017-00988-5
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Junyi Ju Aiping Chen Yexuan Deng Ming Liu Ying Wang Yadong Wang Min Nie Chao Wang Hong Ding Bing Yao Tao Gui Xinyu Li Zhen Xu Chi Ma Yong Song Marc Kvansakul Ke Zen Chen-Yu Zhang Cheng Luo Ming Fang David C. S. Huang C. David Allis Renxiang Tan Changjiang Kathy Zeng Jiwu Wei Quan Zhao
spellingShingle	Junyi Ju Aiping Chen Yexuan Deng Ming Liu Ying Wang Yadong Wang Min Nie Chao Wang Hong Ding Bing Yao Tao Gui Xinyu Li Zhen Xu Chi Ma Yong Song Marc Kvansakul Ke Zen Chen-Yu Zhang Cheng Luo Ming Fang David C. S. Huang C. David Allis Renxiang Tan Changjiang Kathy Zeng Jiwu Wei Quan Zhao NatD promotes lung cancer progression by preventing histone H4 serine phosphorylation to activate Slug expression Nature Communications
author_facet	Junyi Ju Aiping Chen Yexuan Deng Ming Liu Ying Wang Yadong Wang Min Nie Chao Wang Hong Ding Bing Yao Tao Gui Xinyu Li Zhen Xu Chi Ma Yong Song Marc Kvansakul Ke Zen Chen-Yu Zhang Cheng Luo Ming Fang David C. S. Huang C. David Allis Renxiang Tan Changjiang Kathy Zeng Jiwu Wei Quan Zhao
author_sort	Junyi Ju
title	NatD promotes lung cancer progression by preventing histone H4 serine phosphorylation to activate Slug expression
title_short	NatD promotes lung cancer progression by preventing histone H4 serine phosphorylation to activate Slug expression
title_full	NatD promotes lung cancer progression by preventing histone H4 serine phosphorylation to activate Slug expression
title_fullStr	NatD promotes lung cancer progression by preventing histone H4 serine phosphorylation to activate Slug expression
title_full_unstemmed	NatD promotes lung cancer progression by preventing histone H4 serine phosphorylation to activate Slug expression
title_sort	natd promotes lung cancer progression by preventing histone h4 serine phosphorylation to activate slug expression
publisher	Nature Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2017-10-01
description	NatD is an acetyltransferase responsible for N-α-terminal acetylation of the histone H4 and H2A and has been linked to cell growth. Here the authors show that NatD-mediated acetylation of histone H4 serine 1 competes with the phosphorylation by CK2α at the same residue thus leading to the upregulation of Slug and tumor progression.
url	https://doi.org/10.1038/s41467-017-00988-5
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NatD promotes lung cancer progression by preventing histone H4 serine phosphorylation to activate Slug expression

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