Evidence map›Paper›PMID 40022732›Full record

ArticleCell reports2025

RNF10 and RIOK3 facilitate 40S ribosomal subunit degradation upon 60S biogenesis disruption or amino acid starvation.

Pierce W Ford, Danielle M Garshott, Mythreyi Narasimhan, Xuezhen Ge, Eric M Jordahl, Shubha Subramanya, Eric J Bennett

Abstract read
In one paragraph

Article in Cell reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed, 1 pooled it
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
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  7. Ribosome-associated quality control and related mechanisms.Nature structural & molecular biology · 2026
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Pierce W FordSchool of Biological Sciences, Department of Cell and Developmental Biology, University of California, San Diego, La Jolla, CA 92093, USA.
Danielle M GarshottSchool of Biological Sciences, Department of Cell and Developmental Biology, University of California, San Diego, La Jolla, CA 92093, USA.
Mythreyi NarasimhanSchool of Biological Sciences, Department of Cell and Developmental Biology, University of California, San Diego, La Jolla, CA 92093, USA.
Xuezhen GeSchool of Biological Sciences, Department of Cell and Developmental Biology, University of California, San Diego, La Jolla, CA 92093, USA.
Eric M JordahlSchool of Biological Sciences, Department of Cell and Developmental Biology, University of California, San Diego, La Jolla, CA 92093, USA.
Shubha SubramanyaSchool of Biological Sciences, Department of Cell and Developmental Biology, University of California, San Diego, La Jolla, CA 92093, USA.
Eric J BennettSchool of Biological Sciences, Department of Cell and Developmental Biology, University of California, San Diego, La Jolla, CA 92093, USA. Electronic address: e1bennett@ucsd.edu.

Funding

Pathways in Biological Sciences Training ProgramT32GM133351 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Matthew Daugherty, Randolph Y. Hampton · 2020 to 2026
$9.9M
Leveraging ubiquitin-dependent regulatory mechanisms to improve proteome quality in health and diseaseR35GM148339 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Eric J Bennett · 2023 to 2026
$2.1M
Defining the function and mechanism of regulatory ribosomal ubiquitylationR01GM136994 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BENNETT, ERIC J · 2021 to 2023
$1.1M
NIGMS NIH HHS R01 GM136994NIGMS NIH HHS R35 GM148339NIGMS NIH HHS T32 GM133351
6 · The paper itself

Abstract

The initiation-specific ribosome-associated quality control pathway (iRQC) is activated when translation initiation complexes fail to transition to elongation-competent 80S ribosomes. Upon iRQC activation, RNF10 ubiquitylates the 40S proteins uS3 and uS5, which leads to 40S decay. How iRQC is activated in the absence of pharmacological translation inhibitors and what mechanisms govern iRQC capacity and activity remain unanswered questions. Here, we demonstrate that altering 60S:40S stoichiometry by disrupting 60S biogenesis triggers iRQC activation and 40S decay. Depleting the critical scanning helicase eIF4A1 impairs 40S ubiquitylation and degradation, indicating mRNA engagement is required for iRQC. We show that amino acid starvation conditions also stimulate iRQC-dependent 40S decay. We identify RIOK3 as a crucial iRQC factor that interacts with ubiquitylated 40S subunits to mediate degradation. Both RNF10 and RIOK3 protein levels increase upon iRQC pathway activation, establishing a feedforward mechanism that regulates iRQC capacity and subsequent 40S decay.

Indexed as

Amino AcidsRibosome Subunits, Large, EukaryoticRibosome Subunits, Small, EukaryoticSaccharomyces cerevisiae ProteinsUbiquitin-Protein LigasesHumansProteolysisUbiquitinationAmino AcidsSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligases40S degradation60S biogenesisamino acid starvationCP: Molecular biologyiRQCribosomal subunit imbalanceribosomal ubiquitylationRIOK3RNF10

Identifiers

PMID40022732
PMCPMC12008924

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.