RIOK3 mediates the degradation of 40S ribosomes

Cells tightly regulate ribosome homeostasis to adapt to changing environments. Ribosomes are degraded during stress, but the mechanisms responsible remain unclear. Here, we show that starvation induces the selective depletion of 40S ribosomes following their ubiquitylation by the E3 ligase RNF10. The atypical kinase RIOK3 specifically recognizes these ubiquitylated 40S ribosomes through a unique ubiquitin-interacting motif, visualized by cryoelectron microscopy (cryo-EM). RIOK3 binding and ubiquitin recognition are essential for 40S ribosome degradation during starvation. RIOK3 induces the degradation of ubiquitylated 40S ribosomes through progressive decay of their 18S rRNA beginning at the 3' end, as revealed by cryo-EM structures of degradation intermediates. Together, these data define a pathway and mechanism for stress-induced degradation of 40S ribosomes, directly connecting ubiquitylation to regulation of ribosome homeostasis.

Authors

Institutions

Publication Details

Journal
Molecular Cell
Published
2025-02-01
DOI
https://doi.org/10.1016/j.molcel.2025.01.013
Citations
15
Primary Topic
RNA modifications and cancer
Type
article
Field-Weighted Citation Impact
12.09

Funders

Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

RIOK3 mediates the degradation of 40S ribosomes

Roland Beckmann, Mengjiao Wang, Aixia Song, Frances F. Diehl et al.
15 citations
Molecular Cell
RNA modifications and cancer
12.09
article

RIOK3 mediates the degradation of 40S ribosomes

Roland Beckmann, Mengjiao Wang, Aixia Song, Frances F. Diehl, Nicolle A. Rosa-Mercado, Jingdong Cheng, Rachel Green, Fei Chen, Zixuan Huang, Yi Li
article en
15 citations

Abstract

Cells tightly regulate ribosome homeostasis to adapt to changing environments. Ribosomes are degraded during stress, but the mechanisms responsible remain unclear. Here, we show that starvation induces the selective depletion of 40S ribosomes following their ubiquitylation by the E3 ligase RNF10. The atypical kinase RIOK3 specifically recognizes these ubiquitylated 40S ribosomes through a unique ubiquitin-interacting motif, visualized by cryoelectron microscopy (cryo-EM). RIOK3 binding and ubiquitin recognition are essential for 40S ribosome degradation during starvation. RIOK3 induces the degradation of ubiquitylated 40S ribosomes through progressive decay of their 18S rRNA beginning at the 3' end, as revealed by cryo-EM structures of degradation intermediates. Together, these data define a pathway and mechanism for stress-induced degradation of 40S ribosomes, directly connecting ubiquitylation to regulation of ribosome homeostasis.

Molecular CellVol. 85(4)
Howard Hughes Medical Institute (US), Johns Hopkins University (US), Johns Hopkins Medicine (US), Ministry of Science and Technology (LA)
Howard Hughes Medical Institute, Jane Coffin Childs Memorial Fund for Medical Research, National Natural Science Foundation of China, Science and Technology Commission of Shanghai Municipality, Key Technologies Research and Development Program
Openalex Percentile: Top 1%
RNA modifications and cancer
12.09
DOIOpen Access PDFOpenAlex
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.