Datasets

Title	Scope and mechanism of eIF4F-independent mRNA translation
Organism
Number of Samples	7
Release Date	2017/07/25 00:00
Sequencing Types
Protocol Details

Title
Authors	Coots RA,Liu XM,Mao Y,Dong L,Zhou J,Wan J,Zhang X,Qian SB
Journal	Molecular cell
Publication Date	2017 Nov 2
Abstract	In eukaryotic cells, protein synthesis typically begins with the binding of eIF4F to the 7-methylguanylate (m 7 G) cap found on the 5' end of the majority of mRNAs. Surprisingly, overall translational output remains robust under eIF4F inhibition. The broad spectrum of eIF4F-resistant translatomes is incompatible with cap-independent translation mediated by internal ribosome entry sites (IRESs). Here, we report that N 6 -methyladenosine (m 6 A) facilitates mRNA translation that is resistant to eIF4F inactivation. Depletion of the methyltransferase METTL3 selectively inhibits translation of mRNAs bearing 5' UTR methylation, but not mRNAs with 5' terminal oligopyrimidine (TOP) elements. We identify ABCF1 as a critical mediator of m 6 A-promoted translation under both stress and physiological conditions. Supporting the role of ABCF1 in m 6 A-facilitated mRNA translation, ABCF1-sensitive transcripts largely overlap with METTL3-dependent mRNA targets. By illustrating the scope and mechanism of eIF4F-independent mRNA translation, these findings reshape our current perceptions of cellular translational pathways. Copyright © 2017 Elsevier Inc. All rights reserved.
PMC	PMC5913006
PMID	29107534
DOI

Coots et al. 2017 (PRJNA395723)