YTH Domain: A Family of N6-methyladenosine (m6A) Readers
By Shanhui Liao, Hongbin Sun, Chao Xu. Genomics, Proteomics & Bioinformatics, 2018
357 citations recorded by the source corpus.
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.
Subfields: Electrical and Electronic Engineering, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/269892a37cea81e313f9d19566470bbc3c0d5439
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In Molecular Biology
Citations in the corpus
- The m6A reader YTHDF1 promotes ovarian cancer progression via augmenting EIF3C translation (2020, background): “identify the m6A modification and are responsible for the outcomes of m6A-modified mRNAs (9).”
- How RNA binding proteins interact with RNA: molecules and mechanisms (2020, background): “Lastly, many RBPs exhibit neither specific nor high-affinity binding for the purpose of functionally transient associations with RNA (Auweter et al., 2007; Linder and Jankowsky, 2011).”