The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
SUMOylation of the m6A-RNA methyltransferase METTL3 modulates its function
Open accessAbstract
The methyltransferase like 3 (METTL3) is a key component of the large N6-adenosine-methyltransferase complex in mammalian responsible for N6-methyladenosine (m6A) modification in diverse RNAs including mRNA, tRNA, rRNA, small nuclear RNA, microRNA precursor and long non-coding RNA. However, the characteristics of METTL3 in activation and post-translational modification (PTM) is seldom understood. Here we find that METTL3 is modified by SUMO1 mainly at lysine residues K177, K211, K212 and K215, which can be reduced by an SUMO1-specific protease SENP1. SUMOylation of METTL3 does not alter its stability, localization and interaction with METTL14 and WTAP, but significantly represses its m6A methytransferase activity resulting in the decrease of m6A levels in mRNAs. Consistently with this, the abundance of m6A in mRNAs is increased with re-expression of the mutant METTL3-4KR compared to that of wild-type METTL3 in human non-small cell lung carcinoma (NSCLC) cell line H1299-shMETTL3, in which endogenous METTL3 was knockdown. The alternation of m6A in mRNAs and subsequently change of gene expression profiles, which are mediated by SUMOylation of METTL3, may directly influence the soft-agar colony formation and xenografted tumor growth of H1299 cells. Our results uncover an important mechanism for SUMOylation of METTL3 regulating its m6A RNA methyltransferase activity.
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Cites
N6-methyladenosine-dependent regulation of messenger RNA stability
Wang, X., Lu, Z., Gomez, A., Hon, G. C., Yue, Y., Han, D., Fu, Y., Parisien, M., Dai, Q., Jia, G., et al. (2014) · Nature · doi:10.1038/nature12730 · Cited by 4,558
Comprehensive Analysis of mRNA Methylation Reveals Enrichment in 3′ UTRs and near Stop Codons
Meyer, K. D., Saletore, Y., Zumbo, P., Elemento, O., Mason, C. E., & Jaffrey, S. R. (2012) · Cell · doi:10.1016/j.cell.2012.05.003 · Cited by 4,223
N6-Methyladenosine in nuclear RNA is a major substrate of the obesity-associated FTO
Jia, G., Fu, Y., Zhao, X., Dai, Q., Zheng, G., Yang, Y., Yi, C., Lindahl, T., Pan, T., Yang, Y.-G., et al. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.687 · Cited by 4,106
Self-citationALKBH5 Is a Mammalian RNA Demethylase that Impacts RNA Metabolism and Mouse Fertility
Zheng, G., Dahl, J. A., Niu, Y., Fedorcsak, P., Huang, C.-M., Li, C. J., Vågbø, C. B., Shi, Y., Wang, W.-L., Song, S.-H., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.10.015 · Cited by 3,550
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Cited by
The proteins of mRNA modification: writers, readers, and erasers
Flamand, M. N., Tegowski, M., & Meyer, K. D. (2023) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-052521-035330 · Cited by 164
De Jesus, D. F., Zhang, Z., Brown, N. K., Li, X., Xiao, L., Hu, J., Gaffrey, M. J., Fogarty, G., Kahraman, S., Wei, J., et al. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01368-0 · Cited by 56
SUMOylation of the m6A reader YTHDF2 by PIAS1 promotes viral RNA decay to restrict EBV replication
Sugiokto, F. G., Saiada, F., Zhang, K., & Li, R. (2024) · mBio · doi:10.1128/mbio.03168-23 · Cited by 23
Metadata
- Authors
- Du, Y., Hou, G., Zhang, H., Dou, J., He, J., Guo, Y., Li, L., Chen, R., Wang, Y., Deng, R., Huang, J., Jiang, B., Xu, M., Cheng, J., Chen, G.-Q., Zhao, X., & Yu, J.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2018-02-28
- Volume
- 46
- Issue
- 10
- Pages
- 5195-5208
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- OpenAlex
- W2793246329
- Cited by
- 312
- References
- 4
- FWCI
- 8.71
- Type
- journal article
- Language
- en
- Open access
- gold
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- Du, Y., Hou, G., Zhang, H., Dou, J., He, J., Guo, Y., Li, L., Chen, R., Wang, Y., Deng, R., Huang, J., Jiang, B., Xu, M., Cheng, J., Chen, G.-Q., Zhao, X., & Yu, J. (2018). SUMOylation of the m6A-RNA methyltransferase METTL3 modulates its function. Nucleic Acids Research. https://doi.org/10.1093/nar/gky156
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