Cited by 1,815RNA modifications and cancerRNA and protein synthesis mechanismsRNA regulation and disease

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YTHDF3 facilitates translation and decay of N6-methyladenosine-modified RNA

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Shi, Hailing, Wang, Xiao, Lu, Zhike, Zhao, Boxuan S, Ma, Honghui, Hsu, Phillip J, Liu, Chang, He, Chuan·2017·Cell Research

DOI 10.1038/cr.2017.15PMC PMC5339834

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Abstract

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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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
ORCID: Shi, Hailing
Wang, Xiao
Lu, Zhike
Zhao, Boxuan S
Ma, Honghui
Hsu, Phillip J
Liu, Chang
He, Chuan
Venue: Cell Research
Publisher: Springer Science and Business Media LLC
Published: 2017-01-20
Volume: 27
Issue: 3
Pages: 315-328
ISSN: 1001-0602 (ISSN-L)
1748-7838
DOI: 10.1038/cr.2017.15
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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YTHDF3 facilitates translation and decay of N6-methyladenosine-modified RNA

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