Specific sDMA modifications on the RGG/RG motif of METTL14 regulate its function in AML

Abstract Background Protein arginine methylations are crucial post-translational modifications (PTMs) in eukaryotes, playing a significant regulatory role in diverse biological processes. Here, we present our investigation into the detailed arginine methylation pattern of the C-terminal RG-rich regi...

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Main Authors: Yulun Zhong, Rou Zhang, Lingzi Lu, Huijian Tan, Yuyu You, Yang Mao, Yanqiu Yuan
Format: Article
Language:English
Published: BMC 2025-03-01
Series:Cell Communication and Signaling
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Online Access:https://doi.org/10.1186/s12964-025-02130-1
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author Yulun Zhong
Rou Zhang
Lingzi Lu
Huijian Tan
Yuyu You
Yang Mao
Yanqiu Yuan
author_facet Yulun Zhong
Rou Zhang
Lingzi Lu
Huijian Tan
Yuyu You
Yang Mao
Yanqiu Yuan
author_sort Yulun Zhong
collection DOAJ
description Abstract Background Protein arginine methylations are crucial post-translational modifications (PTMs) in eukaryotes, playing a significant regulatory role in diverse biological processes. Here, we present our investigation into the detailed arginine methylation pattern of the C-terminal RG-rich region of METTL14, a key component of the m6A RNA methylation machinery, and its functional implications in biology and disease. Methods Using ETD-based mass spectrometry and in vitro enzyme reactions, we uncover a specific arginine methylation pattern on METTL14. RNA methyltransferase activity assays were used to assess the impact of sDMA on METTL3:METTL14 complex activity. RNA immunoprecipitation was used to evaluate mRNA-m6A reader interactions. MeRIP-seq analysis was used to study the genome-wide effect of METTL14 sDMA on m6A modification in acute myeloid leukemia cells. Results We demonstrate that PRMT5 catalyzes the site-specific symmetric dimethylation at R425 and R445 within the extensively methylated RGG/RG motifs of METTL14. We show a positive regulatory role of symmetric dimethylarginines (sDMA) in the catalytic efficiency of the METTL3:METTL14 complex and m6A-specific gene expression in HEK293T and acute myeloid leukemia cells, potentially through the action of m6A reader protein YTHDF1. In addition, the combined inhibition of METTL3 and PRMT5 further reduces the expression of several m6A substrate genes essential for AML proliferation, suggesting a potential therapeutic strategy for AML treatment. Conclusions The study confirms the coexistence of sDMA and aDMA modifications on METTL14’s RGG/RG motifs, with sDMA at R425 and R445 enhancing METTL3:METTL14’s catalytic efficacy and regulating gene expression through m6A deposition in cancer cells.
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spelling doaj-art-5fd5c53bcf8a4cc28cd3503c23c9e7772025-08-20T01:57:45ZengBMCCell Communication and Signaling1478-811X2025-03-0123111510.1186/s12964-025-02130-1Specific sDMA modifications on the RGG/RG motif of METTL14 regulate its function in AMLYulun Zhong0Rou Zhang1Lingzi Lu2Huijian Tan3Yuyu You4Yang Mao5Yanqiu Yuan6School of Pharmaceutical Sciences, Sun Yat-Sen UniversitySchool of Pharmaceutical Sciences, Sun Yat-Sen UniversitySchool of Pharmaceutical Sciences, Sun Yat-Sen UniversitySchool of Pharmaceutical Sciences, Sun Yat-Sen UniversitySchool of Pharmaceutical Sciences, Sun Yat-Sen UniversitySchool of Pharmaceutical Sciences, Sun Yat-Sen UniversitySchool of Pharmaceutical Sciences, Sun Yat-Sen UniversityAbstract Background Protein arginine methylations are crucial post-translational modifications (PTMs) in eukaryotes, playing a significant regulatory role in diverse biological processes. Here, we present our investigation into the detailed arginine methylation pattern of the C-terminal RG-rich region of METTL14, a key component of the m6A RNA methylation machinery, and its functional implications in biology and disease. Methods Using ETD-based mass spectrometry and in vitro enzyme reactions, we uncover a specific arginine methylation pattern on METTL14. RNA methyltransferase activity assays were used to assess the impact of sDMA on METTL3:METTL14 complex activity. RNA immunoprecipitation was used to evaluate mRNA-m6A reader interactions. MeRIP-seq analysis was used to study the genome-wide effect of METTL14 sDMA on m6A modification in acute myeloid leukemia cells. Results We demonstrate that PRMT5 catalyzes the site-specific symmetric dimethylation at R425 and R445 within the extensively methylated RGG/RG motifs of METTL14. We show a positive regulatory role of symmetric dimethylarginines (sDMA) in the catalytic efficiency of the METTL3:METTL14 complex and m6A-specific gene expression in HEK293T and acute myeloid leukemia cells, potentially through the action of m6A reader protein YTHDF1. In addition, the combined inhibition of METTL3 and PRMT5 further reduces the expression of several m6A substrate genes essential for AML proliferation, suggesting a potential therapeutic strategy for AML treatment. Conclusions The study confirms the coexistence of sDMA and aDMA modifications on METTL14’s RGG/RG motifs, with sDMA at R425 and R445 enhancing METTL3:METTL14’s catalytic efficacy and regulating gene expression through m6A deposition in cancer cells.https://doi.org/10.1186/s12964-025-02130-1METTL14Symmetric dimethylarginineN6-methyladenosinePost-translational modificationAcute myeloid leukemia
spellingShingle Yulun Zhong
Rou Zhang
Lingzi Lu
Huijian Tan
Yuyu You
Yang Mao
Yanqiu Yuan
Specific sDMA modifications on the RGG/RG motif of METTL14 regulate its function in AML
Cell Communication and Signaling
METTL14
Symmetric dimethylarginine
N6-methyladenosine
Post-translational modification
Acute myeloid leukemia
title Specific sDMA modifications on the RGG/RG motif of METTL14 regulate its function in AML
title_full Specific sDMA modifications on the RGG/RG motif of METTL14 regulate its function in AML
title_fullStr Specific sDMA modifications on the RGG/RG motif of METTL14 regulate its function in AML
title_full_unstemmed Specific sDMA modifications on the RGG/RG motif of METTL14 regulate its function in AML
title_short Specific sDMA modifications on the RGG/RG motif of METTL14 regulate its function in AML
title_sort specific sdma modifications on the rgg rg motif of mettl14 regulate its function in aml
topic METTL14
Symmetric dimethylarginine
N6-methyladenosine
Post-translational modification
Acute myeloid leukemia
url https://doi.org/10.1186/s12964-025-02130-1
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