YTH Domain: A Family of N6-methyladenosine (m6A) Readers
Like protein and DNA, different types of RNA molecules undergo various modifications. Accumulating evidence suggests that these RNA modifications serve as sophisticated codes to mediate RNA behaviors and many important biological functions. N6-methyladenosine (m6A) is the most abundant internal RNA...
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| Format: | Article |
| Language: | English |
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Oxford University Press
2018-04-01
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| Series: | Genomics, Proteomics & Bioinformatics |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S1672022918300408 |
| _version_ | 1827160723061473280 |
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| author | Shanhui Liao Hongbin Sun Chao Xu |
| author_facet | Shanhui Liao Hongbin Sun Chao Xu |
| author_sort | Shanhui Liao |
| collection | DOAJ |
| description | Like protein and DNA, different types of RNA molecules undergo various modifications. Accumulating evidence suggests that these RNA modifications serve as sophisticated codes to mediate RNA behaviors and many important biological functions. N6-methyladenosine (m6A) is the most abundant internal RNA modification found in a variety of eukaryotic RNAs, including but not limited to mRNAs, tRNAs, rRNAs, and long non-coding RNAs (lncRNAs). In mammalian cells, m6A can be incorporated by a methyltransferase complex and removed by demethylases, which ensures that the m6A modification is reversible and dynamic. Moreover, m6A is recognized by the YT521-B homology (YTH) domain-containing proteins, which subsequently direct different complexes to regulate RNA signaling pathways, such as RNA metabolism, RNA splicing, RNA folding, and protein translation. Herein, we summarize the recent progresses made in understanding the molecular mechanisms underlying the m6A recognition by YTH domain-containing proteins, which would shed new light on m6A-specific recognition and provide clues to the future identification of reader proteins of many other RNA modifications. Keywords: RNA modification, RNA methylation, RNA demethylation, YT521-B homology, Epitranscriptome |
| first_indexed | 2024-03-08T07:06:14Z |
| format | Article |
| id | doaj.art-f3432a0758c24f9098ddf148b6292b39 |
| institution | Directory Open Access Journal |
| issn | 1672-0229 |
| language | English |
| last_indexed | 2025-03-21T00:17:33Z |
| publishDate | 2018-04-01 |
| publisher | Oxford University Press |
| record_format | Article |
| series | Genomics, Proteomics & Bioinformatics |
| spelling | doaj.art-f3432a0758c24f9098ddf148b6292b392024-08-03T09:01:30ZengOxford University PressGenomics, Proteomics & Bioinformatics1672-02292018-04-0116299107YTH Domain: A Family of N6-methyladenosine (m6A) ReadersShanhui Liao0Hongbin Sun1Chao Xu2Heifei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei 230027, ChinaSchool of Food and Biological Engineering, Zhengzhou University of Light Industry, Zhengzhou 450002, China; Corresponding authors.Heifei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei 230027, China; CAS Key Laboratory of Structural Biology, University of Science and Technology of China, Hefei 230027, China; Corresponding authors.Like protein and DNA, different types of RNA molecules undergo various modifications. Accumulating evidence suggests that these RNA modifications serve as sophisticated codes to mediate RNA behaviors and many important biological functions. N6-methyladenosine (m6A) is the most abundant internal RNA modification found in a variety of eukaryotic RNAs, including but not limited to mRNAs, tRNAs, rRNAs, and long non-coding RNAs (lncRNAs). In mammalian cells, m6A can be incorporated by a methyltransferase complex and removed by demethylases, which ensures that the m6A modification is reversible and dynamic. Moreover, m6A is recognized by the YT521-B homology (YTH) domain-containing proteins, which subsequently direct different complexes to regulate RNA signaling pathways, such as RNA metabolism, RNA splicing, RNA folding, and protein translation. Herein, we summarize the recent progresses made in understanding the molecular mechanisms underlying the m6A recognition by YTH domain-containing proteins, which would shed new light on m6A-specific recognition and provide clues to the future identification of reader proteins of many other RNA modifications. Keywords: RNA modification, RNA methylation, RNA demethylation, YT521-B homology, Epitranscriptomehttp://www.sciencedirect.com/science/article/pii/S1672022918300408 |
| spellingShingle | Shanhui Liao Hongbin Sun Chao Xu YTH Domain: A Family of N6-methyladenosine (m6A) Readers Genomics, Proteomics & Bioinformatics |
| title | YTH Domain: A Family of N6-methyladenosine (m6A) Readers |
| title_full | YTH Domain: A Family of N6-methyladenosine (m6A) Readers |
| title_fullStr | YTH Domain: A Family of N6-methyladenosine (m6A) Readers |
| title_full_unstemmed | YTH Domain: A Family of N6-methyladenosine (m6A) Readers |
| title_short | YTH Domain: A Family of N6-methyladenosine (m6A) Readers |
| title_sort | yth domain a family of n6 methyladenosine m6a readers |
| url | http://www.sciencedirect.com/science/article/pii/S1672022918300408 |
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