Evidence map›Paper›PMID 27325745›Full record

ArticleNucleic acids research2016

Distinct types of translation termination generate substrates for ribosome-associated quality control.

Natalia Shcherbik, Tatiana A Chernova, Yury O Chernoff, Dimitri G Pestov

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

17 citing papers in PubMed, 19 citations in OpenAlex.

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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

4 authors at 3 institutions in 2 countries.

Natalia ShcherbikDepartment of Cell Biology, Rowan University, School of Osteopathic Medicine, Stratford, NJ 08084, USA shcherna@rowan.edu.ORCID 0000-0002-2127-8939
Tatiana A ChernovaDepartment of Biochemistry, Emory University, School of Medicine, Atlanta, GA 30322, USA.
Yury O ChernoffSchool of Biology, Georgia Institute of Technology, Atlanta, GA 30322, USA Laboratory of Amyloid Biology & Institute of Translational Biomedicine, St. Petersburg State University, St. Petersburg 199034, Russia.
Dimitri G PestovDepartment of Cell Biology, Rowan University, School of Osteopathic Medicine, Stratford, NJ 08084, USA.ORCID 0000-0002-1425-9879
Rowan University · USEmory University · USGeorgia Institute of Technology · US

Funding

Monitoring mechanisms in mammalian ribosome biogenesisR01GM074091 · NIGMS · UNIV OF MED/DENT NJ-SCH OSTEOPATHIC MED · PI PESTOV, DIMITRI G · 2005 to 2014
$2.4M
Ubiquitin and regulation of prion induction by a short-lived proteinR01GM093294 · NIGMS · EMORY UNIVERSITY · PI WILKINSON, KEITH D · 2011 to 2014
$1.3M
NIGMS NIH HHS R01 GM074091NIGMS NIH HHS R01 GM093294
6 · The paper itself

Abstract

Cotranslational degradation of polypeptide nascent chains plays a critical role in quality control of protein synthesis and the rescue of stalled ribosomes. In eukaryotes, ribosome stalling triggers release of 60S subunits with attached nascent polypeptides, which undergo ubiquitination by the E3 ligase Ltn1 and proteasomal degradation facilitated by the ATPase Cdc48. However, the identity of factors acting upstream in this process is less clear. Here, we examined how the canonical release factors Sup45-Sup35 (eRF1-eRF3) and their paralogs Dom34-Hbs1 affect the total population of ubiquitinated nascent chains associated with yeast ribosomes. We found that the availability of the functional release factor complex Sup45-Sup35 strongly influences the amount of ubiquitinated polypeptides associated with 60S ribosomal subunits, while Dom34-Hbs1 generate 60S-associated peptidyl-tRNAs that constitute a relatively minor fraction of Ltn1 substrates. These results uncover two separate pathways that target nascent polypeptides for Ltn1-Cdc48-mediated degradation and suggest that in addition to canonical termination on stop codons, eukaryotic release factors contribute to cotranslational protein quality control.

Indexed as

Models, BiologicalMolecular WeightPeptide Chain Termination, TranslationalPeptidesRibosomesRibosome Subunits, Large, EukaryoticSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinUbiquitinationUbiquitin-Protein LigasesPeptidesSaccharomyces cerevisiae ProteinsUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID27325745
PMCPMC5001609
OpenAlexW2468874056

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.