The E3 ubiquitin ligase RNF10 modifies 40S ribosomal subunits of ribosomes compromised in translation

Abstract

The E3 ubiquitin ligase RNF10 modifies 40S ribosomal subunits of ribosomes compromised in translation Graphical abstract Highlights d RNF10 monoubiquitinates ribosomal proteins RPS2 and RPS3 d RNF10 crosslinks to mRNA 5 0 UTR and coding sequences, tRNAs, and rRNAs d Monoubiquitination flags ribosomes arrested in translation initiation or elongation d This monoubiquitination is reversed by USP10 during recycling of stalled ribosomes

Sensing of individual stalled 80S ribosomes by Fap1 for nonfunctional rRNA turnover

“…Since the codon recognition process is highly conserved and there are putative homologs of yeast 18S NRD factors in mammals (Garshott et al, 2021;Garzia et al, 2021;Kunz et al, 2000), it is conceivable that mammalian cells had to evolve similar systems that broaden the ability to handle diverse translational aberrancy.…”

Ubiquitin-mediated mechanisms of translational control

“…On the contrary, if these modifications are eliminated by deubiquitinase USP10, translation and protein synthesis are resumed (Fig. 2A) [61,62].…”

Ubiquitination of stalled ribosomes enables mRNA decay via HBS-1 and NONU-1in vivo

“…The copyright holder for this preprint this version posted November 8, 2021. ; https://doi.org/10.1101/2021.11.08.467757 doi: bioRxiv preprint future work will hopefully clarify the recruitment mechanisms of each (Ikeuchi et al, 2019;Garzia and Meyer et al, 2021).…”

“…Given that there are structural differences in collided ribosome conformation during Nonstop mRNA Decay vs. No-Go mRNA Decay (Hilal et al, 2016;Becker et al, 2011), we hypothesize that an E3 ligase other than ZNF-598 is better equipped to recognize ribosomes stalled at the 3'end of an mRNA and trigger Nonstop mRNA Decay. Other E3 ligases have been implicated in surveillance, such as Not4 and RNF10, and future work will hopefully clarify the recruitment mechanisms of each (Ikeuchi et al, 2019;Garzia and Meyer et al, 2021).…”