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Tytuł:
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Arginine methylation of METTL14 promotes RNA N -methyladenosine modification and endoderm differentiation of mouse embryonic stem cells.
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Autorzy:
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Liu X; School of Life Sciences, University of Science and Technology of China, Hefei, P.R. China.; Department of Developmental Biology, School of Basic Medical Sciences, Southern Medical University, Guangzhou, P.R. China.; State Key Laboratory of Reproductive Biology, Institute of Zoology, Chinese Academy of Sciences, Beijing, China.
Wang H; Kingmed School of Laboratory Medicine, Guangzhou Medical University, Guangzhou, P.R. China.
Zhao X; Department of Developmental Biology, School of Basic Medical Sciences, Southern Medical University, Guangzhou, P.R. China.
Luo Q; Department of Forensic Toxicology, School of Forensic Medicine, Southern Medical University, Guangzhou, P.R. China.
Wang Q; Department of Developmental Biology, School of Basic Medical Sciences, Southern Medical University, Guangzhou, P.R. China.
Tan K; Department of Developmental Biology, School of Basic Medical Sciences, Southern Medical University, Guangzhou, P.R. China.
Wang Z; Department of Developmental Biology, School of Basic Medical Sciences, Southern Medical University, Guangzhou, P.R. China.
Jiang J; Department of Developmental Biology, School of Basic Medical Sciences, Southern Medical University, Guangzhou, P.R. China.
Cui J; Department of Developmental Biology, School of Basic Medical Sciences, Southern Medical University, Guangzhou, P.R. China.
Du E; Department of Developmental Biology, School of Basic Medical Sciences, Southern Medical University, Guangzhou, P.R. China.
Xia L; Department of Developmental Biology, School of Basic Medical Sciences, Southern Medical University, Guangzhou, P.R. China.
Du W; Sichuan MoDe Technology Co., Ltd, Chengdu, P. R. China.
Chen D; State Key Laboratory of Reproductive Biology, Institute of Zoology, Chinese Academy of Sciences, Beijing, China. .; Institute of Biomedical Research, Yunnan University, Kunming, P.R. China. .
Xia L; Department of Developmental Biology, School of Basic Medical Sciences, Southern Medical University, Guangzhou, P.R. China. .; State Key Laboratory of Organ Failure Research, Southern Medical University, Guangzhou, P.R. China. .
Xiao S; Department of Developmental Biology, School of Basic Medical Sciences, Southern Medical University, Guangzhou, P.R. China. .
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Źródło:
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Nature communications [Nat Commun] 2021 Jun 18; Vol. 12 (1), pp. 3780. Date of Electronic Publication: 2021 Jun 18.
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Typ publikacji:
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Journal Article; Research Support, Non-U.S. Gov't
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Język:
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English
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Imprint Name(s):
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Original Publication: [London] : Nature Pub. Group
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MeSH Terms:
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Adenosine/*analogs & derivatives
Arginine/*metabolism
Endoderm/*cytology
Methyltransferases/*metabolism
Mouse Embryonic Stem Cells/*cytology
Adenosine/genetics ; Adenosine/metabolism ; Animals ; Cell Differentiation/genetics ; Gene Expression Regulation/genetics ; HEK293 Cells ; HeLa Cells ; Humans ; Methylation ; Methyltransferases/genetics ; Mice ; Protein Processing, Post-Translational/genetics ; Protein-Arginine N-Methyltransferases/genetics ; Protein-Arginine N-Methyltransferases/metabolism ; RNA Interference ; RNA, Small Interfering/genetics
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Substance Nomenclature:
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0 (RNA, Small Interfering)
94ZLA3W45F (Arginine)
CLE6G00625 (N-methyladenosine)
EC 2.1.1.- (Methyltransferases)
EC 2.1.1.- (Mettl14 protein, mouse)
EC 2.1.1.- (Mettl3 protein, mouse)
EC 2.1.1.319 (Prmt1 protein, mouse)
EC 2.1.1.319 (Protein-Arginine N-Methyltransferases)
K72T3FS567 (Adenosine)
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Entry Date(s):
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Date Created: 20210619 Date Completed: 20210706 Latest Revision: 20240402
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Update Code:
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20240402
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PubMed Central ID:
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PMC8213825
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DOI:
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10.1038/s41467-021-24035-6
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PMID:
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34145242
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RNA N 6 -methyladenosine (m 6 A), the most abundant internal modification of mRNAs, plays key roles in human development and health. Post-translational methylation of proteins is often critical for the dynamic regulation of enzymatic activity. However, the role of methylation of the core methyltransferase METTL3/METTL14 in m 6 A regulation remains elusive. We find by mass spectrometry that METTL14 arginine 255 (R255) is methylated (R255me). Global mRNA m 6 A levels are greatly decreased in METTL14 R255K mutant mouse embryonic stem cells (mESCs). We further find that R255me greatly enhances the interaction of METTL3/METTL14 with WTAP and promotes the binding of the complex to substrate RNA. We show that protein arginine N-methyltransferases 1 (PRMT1) interacts with and methylates METTL14 at R255, and consistent with this, loss of PRMT1 reduces mRNA m 6 A modification globally. Lastly, we find that loss of R255me preferentially affects endoderm differentiation in mESCs. Collectively, our findings show that arginine methylation of METTL14 stabilizes the binding of the m 6 A methyltransferase complex to its substrate RNA, thereby promoting global m 6 A modification and mESC endoderm differentiation. This work highlights the crosstalk between protein methylation and RNA methylation in gene expression.