The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
YTHDF2 destabilizes m6A-containing RNA through direct recruitment of the CCR4–NOT deadenylase complex
Open accessAbstract
Methylation at the N 6 position of adenosine (m 6 A) is the most abundant RNA modification within protein-coding and long noncoding RNAs in eukaryotes and is a reversible process with important biological functions. YT521-B homology domain family (YTHDF) proteins are the readers of m 6 A, the binding of which results in the alteration of the translation efficiency and stability of m 6 A-containing RNAs. However, the mechanism by which YTHDF proteins cause the degradation of m 6 A-containing RNAs is poorly understood. Here we report that m 6 A-containing RNAs exhibit accelerated deadenylation that is mediated by the CCR4–NOT deadenylase complex. We further show that YTHDF2 recruits the CCR4–NOT complex through a direct interaction between the YTHDF2 N-terminal region and the SH domain of the CNOT1 subunit, and that this recruitment is essential for the deadenylation of m 6 A-containing RNAs by CAF1 and CCR4. Therefore, we have uncovered the mechanism of YTHDF2-mediated degradation of m 6 A-containing RNAs in mammalian cells.
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Cites
Functions of DNA methylation: islands, start sites, gene bodies and beyond
Jones, P. A. (2012) · Nature Reviews Genetics · doi:10.1038/nrg3230 · Cited by 6,061
N6-methyladenosine-dependent regulation of messenger RNA stability
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Comprehensive Analysis of mRNA Methylation Reveals Enrichment in 3′ UTRs and near Stop Codons
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N6-Methyladenosine in nuclear RNA is a major substrate of the obesity-associated FTO
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ALKBH5 Is a Mammalian RNA Demethylase that Impacts RNA Metabolism and Mouse Fertility
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N6-methyladenosine Modulates Messenger RNA Translation Efficiency
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A METTL3–METTL14 complex mediates mammalian nuclear RNA N6-adenosine methylation
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Nuclear m6A Reader YTHDC1 Regulates mRNA Splicing
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Self-citationZebrafish MiR-430 Promotes Deadenylation and Clearance of Maternal mRNAs
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Cited by
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Huang, H., Weng, H., Sun, W., Qin, X., Shi, H., Wu, H., Zhao, B. S., Mesquita, A., Liu, C., Yuan, C. L., et al. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0045-z · Cited by 2,997
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Zaccara, S., Ries, R. J., & Jaffrey, S. R. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0168-5 · Cited by 2,597
The role of m6A modification in the biological functions and diseases
Jiang, X., Liu, B., Nie, Z., Duan, L., Xiong, Q., Jin, Z., Yang, C., & Chen, Y. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00450-x · Cited by 2,335
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Barbieri, I., & Kouzarides, T. (2020) · Nature Reviews Cancer · doi:10.1038/s41568-020-0253-2 · Cited by 1,312
YTHDC1 mediates nuclear export of N6-methyladenosine methylated mRNAs
Roundtree, I. A., Luo, G.-Z., Zhang, Z., Wang, X., Zhou, T., Cui, Y., Sha, J., Huang, X., Guerrero, L., Xie, P., et al. (2017) · eLife · doi:10.7554/elife.31311 · Cited by 1,256
Metadata
- Authors
- Du, H., Zhao, Y., He, J., Zhang, Y., Xi, H., Liu, M., Ma, J., & Wu, L.
- Venue
- Nature Communications
- Published
- 2016-08-25
- Volume
- 7
- Issue
- 1
- Pages
- 12626-12626
- ISSN
- 2041-1723 (ISSN-L)
- OpenAlex
- W2507685096
- Cited by
- 1,463
- References
- 12
- FWCI
- 29.49
- Type
- journal article
- Language
- en
- Open access
- gold
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- Du, H., Zhao, Y., He, J., Zhang, Y., Xi, H., Liu, M., Ma, J., & Wu, L. (2016). YTHDF2 destabilizes m6A-containing RNA through direct recruitment of the CCR4–NOT deadenylase complex. Nature Communications. https://doi.org/10.1038/ncomms12626
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