The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
A Unified Model for the Function of YTHDF Proteins in Regulating m6A-Modified mRNA
Open accessAbstract
Summary N6-methyladenosine (m6A) is the most abundant mRNA nucleotide modification and regulates critical aspects of cellular physiology and differentiation. m6A is thought to mediate its effects through a complex network of interactions between different m6A sites and three functionally distinct cytoplasmic YTHDF m6A-binding proteins (DF1, DF2, and DF3). In contrast to the prevailing model, we show that DF proteins bind the same m6A-modified mRNAs, rather than different mRNAs. Furthermore, we find that DF proteins do not induce translation in HeLa cells. Instead, the DF paralogs act redundantly to mediate mRNA degradation and cellular differentiation. The ability of DF proteins to regulate stability and differentiation becomes evident only when all three DF paralogs are simultaneously depleted. Our studies reveal a unified model of m6A function in which all m6A-modified mRNAs are subjected to the combined action of the YTHDF proteins in proportion to the number of m6A sites.
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Self-citationYTHDF3 facilitates translation and decay of N6-methyladenosine-modified RNA
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Self-citationSingle-nucleotide-resolution mapping of m6A and m6Am throughout the transcriptome
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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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m6A RNA methylation regulates the fate of endogenous retroviruses
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Context-dependent functional compensation between Ythdf m6A reader proteins
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Metadata
- Authors
- Zaccara, S., & Jaffrey, S. R.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2020-06
- Volume
- 181
- Issue
- 7
- Pages
- 1582-1595.e18
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W3029046617
- Cited by
- 797
- References
- 10
- FWCI
- 31.39
- Type
- journal article
- Language
- en
- Open access
- bronze
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