Evidence map›Paper›PMID 27552055›Full record

ArticleeLife2016

A conserved quality-control pathway that mediates degradation of unassembled ribosomal proteins.

Min-Kyung Sung, Tanya R Porras-Yakushi, Justin M Reitsma, Ferdinand M Huber, Michael J Sweredoski, André Hoelz, Sonja Hess, Raymond J Deshaies

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 132 papers.

0numbers the graph read from it
0cells of the map it votes in
132citing papers in PubMed
12.0field-weighted citation impact, top 1% of its field
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

132 citing papers in PubMed, 206 citations in OpenAlex.

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  18. Ribosome-associated proteins: unwRAPping ribosome heterogeneity in the twenty-first century.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
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72 more citing papers are in PubMed but not listed here.

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

8 authors at 1 institution in 1 country.

Min-Kyung SungDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, United States.ORCID 0000-0002-0513-6834
Tanya R Porras-YakushiProteome Exploration Laboratory, Division of Biology and Biological Engineering, Beckman Institue, California Institute of Technology, Pasadena, United States.
Justin M ReitsmaDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, United States.
Ferdinand M HuberDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, United States.
Michael J SweredoskiProteome Exploration Laboratory, Division of Biology and Biological Engineering, Beckman Institue, California Institute of Technology, Pasadena, United States.
André HoelzDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, United States.
Sonja HessProteome Exploration Laboratory, Division of Biology and Biological Engineering, Beckman Institue, California Institute of Technology, Pasadena, United States.
Raymond J DeshaiesDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, United States.ORCID 0000-0002-3671-9354
California Institute of Technology · US

Funding

Molecular Basis of mRNA ExportR01GM117360 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI Andre Hoelz · 2016 to 2026
$2.6M
Mapping the dynamic assembly of SCF E3 ubiquitin ligases during the cell cycleF32GM112308 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI REITSMA, JUSTIN · 2014 to 2016
$157k
Howard Hughes Medical InstituteNIGMS NIH HHS F32 GM112308NIGMS NIH HHS R01 GM117360
6 · The paper itself

Abstract

Overproduced yeast ribosomal protein (RP) Rpl26 fails to assemble into ribosomes and is degraded in the nucleus/nucleolus by a ubiquitin-proteasome system quality control pathway comprising the E2 enzymes Ubc4/Ubc5 and the ubiquitin ligase Tom1. tom1 cells show reduced ubiquitination of multiple RPs, exceptional accumulation of detergent-insoluble proteins including multiple RPs, and hypersensitivity to imbalances in production of RPs and rRNA, indicative of a profound perturbation to proteostasis. Tom1 directly ubiquitinates unassembled RPs primarily via residues that are concealed in mature ribosomes. Together, these data point to an important role for Tom1 in normal physiology and prompt us to refer to this pathway as ERISQ, for excess ribosomal protein quality control. A similar pathway, mediated by the Tom1 homolog Huwe1, restricts accumulation of overexpressed hRpl26 in human cells. We propose that ERISQ is a key element of the quality control machinery that sustains protein homeostasis and cellular fitness in eukaryotes.

Indexed as

Metabolic Networks and PathwaysProteolysisGene DeletionQuality ControlRibosomal ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTumor Suppressor ProteinsUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesHUWE1 protein, humanRibosomal ProteinsRPL26A protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTOM1 protein, S cerevisiaeTumor Suppressor ProteinsUbc4 protein, S cerevisiaeUBC5 protein, S cerevisiaeUbiquitin-Conjugating EnzymesUbiquitin-Protein Ligasesbiochemistrycell biologyhumanprotein quality controlribosomal proteinS. cerevisiaeubiquitin-proteasome system

Identifiers

PMID27552055
PMCPMC5026473
OpenAlexW2511774689

What OpenQuestion holds

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LicenceCC BY
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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.