Evidence map›Paper›PMID 32099016›Full record

ArticleScientific reports2020

Identification of a novel trigger complex that facilitates ribosome-associated quality control in mammalian cells.

Satoshi Hashimoto, Takato Sugiyama, Reina Yamazaki, Risa Nobuta, Toshifumi Inada

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

66 citing papers in PubMed, 111 citations in OpenAlex.

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  5. Ribosome-associated quality control and related mechanisms.Nature structural & molecular biology · 2026
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6 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

5 authors at 1 institution in 1 country.

Satoshi Hashimoto *From the Graduate School of Pharmaceutical Sciences, Tohoku University, Sendai, 980-8578, Japan.
Takato Sugiyama *From the Graduate School of Pharmaceutical Sciences, Tohoku University, Sendai, 980-8578, Japan.
Reina YamazakiFrom the Graduate School of Pharmaceutical Sciences, Tohoku University, Sendai, 980-8578, Japan.
Risa NobutaFrom the Graduate School of Pharmaceutical Sciences, Tohoku University, Sendai, 980-8578, Japan.
Toshifumi InadaFrom the Graduate School of Pharmaceutical Sciences, Tohoku University, Sendai, 980-8578, Japan. toshifumi.inada.a3@tohoku.ac.jp.
Tohoku University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ribosome stalling triggers the ribosome-associated quality control (RQC) pathway, which targets collided ribosomes and leads to subunit dissociation, followed by proteasomal degradation of the nascent peptide. In yeast, RQC is triggered by Hel2-dependent ubiquitination of uS10, followed by subunit dissociation mediated by the RQC-trigger (RQT) complex. In mammals, ZNF598-dependent ubiquitination of collided ribosomes is required for RQC, and activating signal cointegrator 3 (ASCC3), a component of the ASCC complex, facilitates RQC. However, the roles of other components and associated factors of the ASCC complex remain unknown. Here, we demonstrate that the human RQC-trigger (hRQT) complex, an ortholog of the yeast RQT complex, plays crucial roles in RQC. The hRQT complex is composed of ASCC3, ASCC2, and TRIP4, which are orthologs of the RNA helicase Slh1(Rqt2), ubiquitin-binding protein Cue3(Rqt3), and zinc-finger type protein yKR023W(Rqt4), respectively. The ATPase activity of ASCC3 and the ubiquitin-binding activity of ASCC2 are crucial for triggering RQC. Given the proposed function of the RQT complex in yeast, we propose that the hRQT complex recognizes the ubiquitinated stalled ribosome and induces subunit dissociation to facilitate RQC.

Indexed as

DNA HelicasesHEK293 CellsHumansMultiprotein ComplexesNuclear ProteinsRibosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsASCC2 protein, humanASCC3 protein, humanDNA HelicasesMultiprotein ComplexesNuclear ProteinsSaccharomyces cerevisiae ProteinsTranscription FactorsTRIP4 protein, human

Identifiers

PMID32099016
PMCPMC7042231
OpenAlexW3007950993

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.