YTHDF3 facilitates translation and decay of N6-methyladenosine-modified RNA
Open accessAbstract
N 6-methyladenosine (m 6 A) is the most abundant internal modification in eukaryotic messenger RNAs (mRNAs), and plays important roles in cell differentiation and tissue development. It regulates multiple steps throughout the RNA life cycle including RNA processing, translation, and decay, via the recognition by selective binding proteins. In the cytoplasm, m 6 A binding protein YTHDF1 facilitates translation of m 6 A-modified mRNAs, and YTHDF2 accelerates the decay of m 6 A-modified transcripts. The biological function of YTHDF3, another cytoplasmic m 6 A binder of the YTH (YT521-B homology) domain family, remains unknown. Here, we report that YTHDF3 promotes protein synthesis in synergy with YTHDF1, and affects methylated mRNA decay mediated through YTHDF2. Cells deficient in all three YTHDF proteins experience the most dramatic accumulation of m 6 A-modified transcripts. These results indicate that together with YTHDF1 and YTHDF2, YTHDF3 plays critical roles to accelerate metabolism of m 6 A-modified mRNAs in the cytoplasm. All three YTHDF proteins may act in an integrated and cooperative manner to impact fundamental biological processes related to m 6 A RNA methylation.
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Synergistic interactions between YTHDF1 and YTHDF3 allow recognition of m6A in the 3′UTR to facilitate translation.
“m6A modifications in the 3′UTR are recognized by YTHDF2 to regulate mRNA degradation (Wang et al., 2014), while synergistic interactions between YTHDF1 and YTHDF3 allow recognition of m6A in the 3′UTR to facilitate translation (Wang and Roundtree, 2015; Shi et al., 2017).”
From METTL3 uncouples chromatin accessibility from transcription during retinal development (2025) · cites this paper as Shi et al., 2017
The ‘YTHDF3 facilitates translation’ section reports that YTHDF3 amplified YTHDF1’s translation-promoting effect in a 3′-UTR tethering assay. But that assay replaced the proteins’ m6A-binding domains with artificial tethering domains, so it does not directly show that their interaction recognizes m6A in the 3′UTR. (LLM, conf=0.84)
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- Authors
- Shi, H., Wang, X., Lu, Z., Zhao, B. S., Ma, H., Hsu, P. J., Liu, C., & He, C.
- Affiliations
- Howard Hughes Medical Institute (US)
- Corresponding author
- He, Chuan
- Venue
- Cell Research
- Published
- 2017-01-20
- Volume
- 27
- Issue
- 3
- Pages
- 315-328
- ISSN
- 1001-0602 (ISSN-L)
- 1748-7838
- PMC
- PMC5339834
- OpenAlex
- W2575691519
- Cited by
- 1,815
- References
- 55
- Citations by year
- 2026: 132 · 2025: 194 · 2024: 255 · 2023: 272 · 2022: 280 · 2021: 266 · 2020: 192 · 2019: 107 · 2018: 82 · 2017: 35
- FWCI
- 46.49
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Cell Research (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation (1048528)
- Howard Hughes Medical Institute
- University of Chicago
- Fudan University
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM071440, R01GM113194)
- Division of Chemistry (CHE-1048528)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA regulation and disease
- Keywords
- YTHDF3, N6-methyladenosine, m6A RNA methylation, mRNA translation, mRNA degradation, YTHDF1, YTHDF2, YTH domain proteins
- MeSH terms
- Adenosine, Base Sequence, Cytosol, HeLa Cells, Humans, Models, Biological, Protein Binding, RNA, Protein Biosynthesis, RNA-Binding Proteins, RNA Stability
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