Evidence map›Paper›PMID 27481473›Full record

ArticleScientific reports2016

Quality control of nonstop membrane proteins at the ER membrane and in the cytosol.

Shunsuke Arakawa, Kaori Yunoki, Toshiaki Izawa, Yasushi Tamura, Shuh-Ichi Nishikawa, Toshiya Endo

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

33 citing papers in PubMed, 48 citations in OpenAlex.

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  14. RPL26/uL24 UFMylation is essential for ribosome-associated quality control at the endoplasmic reticulum.Proceedings of the National Academy of Sciences of the United States of America · 2023
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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

6 authors at 2 institutions in 1 country.

Shunsuke ArakawaDepartment of Chemistry, Graduate School of Science, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan.
Kaori YunokiFaculty of Life Sciences, Kyoto Sangyo University, Kamigamo-motoyama, Kita-ku, Kyoto 603-8555, Japan.
Toshiaki IzawaDepartment of Chemistry, Graduate School of Science, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan.
Yasushi TamuraResearch Center for Materials Science, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan.
Shuh-Ichi NishikawaDepartment of Chemistry, Graduate School of Science, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan.
Toshiya EndoDepartment of Chemistry, Graduate School of Science, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan.
Nagoya University · JPKyoto Sangyo University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Since messenger RNAs without a stop codon (nonstop mRNAs) for organelle-targeted proteins and their translation products (nonstop proteins) generate clogged translocon channels as well as stalled ribosomes, cells have mechanisms to degrade nonstop mRNAs and nonstop proteins and to clear the translocons (e.g. the Sec61 complex) by release of nonstop proteins into the organellar lumen. Here we followed the fate of nonstop endoplasmic reticulum (ER) membrane proteins with different membrane topologies in yeast to evaluate the importance of the Ltn1-dependent cytosolic degradation and the Dom34-dependent release of the nonstop membrane proteins. Ltn1-dependent degradation differed for membrane proteins with different topologies and its failure did not affect ER protein import or cell growth. On the other hand, failure in the Dom34-dependent release of the nascent polypeptide from the ribosome led to the block of the Sec61 channel and resultant inhibition of other protein import into the ER caused cell growth defects. Therefore, the nascent chain release from the translation apparatus is more instrumental in clearance of the clogged ER translocon channel and thus maintenance of normal cellular functions.

Indexed as

Cell Cycle ProteinsCytosolEndoplasmic ReticulumEndoribonucleasesGTP-Binding ProteinsHSP70 Heat-Shock ProteinsMembrane ProteinsPeptide Elongation FactorsProteasome Endopeptidase ComplexProtein TransportProteolysisRNA, MessengerRNA StabilitySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSEC Translocation ChannelsCell Cycle ProteinsDom34 protein, S cerevisiaeEndoribonucleasesGTP-Binding ProteinsHBS1 protein, S cerevisiaeHSP70 Heat-Shock ProteinsLtn1 protein, S cerevisiaeMembrane ProteinsPeptide Elongation FactorsProteasome Endopeptidase ComplexRNA, MessengerSaccharomyces cerevisiae ProteinsSEC Translocation ChannelsUbiquitin-Protein Ligases

Identifiers

PMID27481473
PMCPMC4969602
OpenAlexW2504235585

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.