Dali Han

TL;DR: It is shown that m6A is selectively recognized by the human YTH domain family 2 (YTHDF2) ‘reader’ protein to regulate mRNA degradation and established the role of YTH DF2 in RNA metabolism, showing that binding of Y THDF2 results in the localization of bound mRNA from the translatable pool to mRNA decay sites, such as processing bodies.

TL;DR: In a unified mechanism of m(6)A-based regulation in the cytoplasm, YTHDF2-mediated degradation controls the lifetime of target transcripts, whereasYTHDF1-mediated translation promotion increases translation efficiency, ensuring effective protein production from dynamic transcripts that are marked by m( 6)A.

TL;DR: It is reported here that human METTL14 catalyzes m6A RNA methylation, and together with METTL3, the only previously known m 6A methyltransferase, these two proteins form a stable heterodimer core complex ofMETTL3-14 that functions in cellular m6 a deposition on mammalian nuclear RNAs.

TL;DR: It is shown that m1A is enriched around the start codon upstream of the first splice site: it preferentially decorates more structured regions around canonical and alternative translation initiation sites, is dynamic in response to physiological conditions, and correlates positively with protein production.

TL;DR: It is shown that durable neoantigen-specific immunity is regulated by mRNA N6-methyadenosine (m6A) methylation through the m6A-binding protein YTHDF15, which suppresses the clearance of tumours by enhancing the translation of lysosomal proteases in dendritic cells and thereby suppressing tumour antigen presentation.