Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2022 Mar 14;10:819044. doi: 10.3389/fcell.2022.819044

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

Copyright © 2022 Chang, Yi, Wang, Cao, Zhou, Ge, Muhammad, Zhang, Feng, Yan, Felici, Shen and Cao.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

PMC Copyright notice

The molecular mechanisms of how m⁶A affects splicing/polyadenylation/translation. YTHDF1 and YTHDF3 regulate m⁶A both individually and together. hnRNPG binds to m⁶A-containing 3′-terminal mRNA and interacts with 40S and 60S ribosomal subunits to regulate mRNA translation, and YTHDF3 also facilitates this process. hnRNPG binds to m6a-containing pre-mRNA and interacts with RNA polymerase II (RNAP II) phosphorylated carboxy-terminal domain (CTD) of RNA polymerase II, which in turn regulates alternative splicing of mRNAs. C-YTHDF2 selectively recognizes m⁶A-containing mRNAs, while N-YTHDF2 on the other side binds to mRNA decay machineries and regulates mRNA degradation. YTH domain binds to the m⁶A-containing pre-mRNA and regulates the length of the 3′ UTR through polyadenylation complexes.