Evidence map›Paper›PMID 33184379›Full record

ArticleScientific reports2020

Ribosomal protein S7 ubiquitination during ER stress in yeast is associated with selective mRNA translation and stress outcome.

Yasuko Matsuki, Yoshitaka Matsuo, Yu Nakano, Shintaro Iwasaki, Hideyuki Yoko, Tsuyoshi Udagawa, Sihan Li, Yasushi Saeki, Tohru Yoshihisa, Keiji Tanaka and 2 more

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 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

25 citing papers in PubMed, 41 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

12 authors at 5 institutions in 2 countries.

Yasuko MatsukiGraduate School of Pharmaceutical Sciences, Tohoku University, Sendai, 980-8578, Japan.
Yoshitaka MatsuoGraduate School of Pharmaceutical Sciences, Tohoku University, Sendai, 980-8578, Japan.
Yu NakanoGraduate School of Pharmaceutical Sciences, Tohoku University, Sendai, 980-8578, Japan.
Shintaro IwasakiDepartment of Molecular and Cell Biology, University of California, Berkeley, CA94720, USA.
Hideyuki YokoGraduate School of Pharmaceutical Sciences, Tohoku University, Sendai, 980-8578, Japan.
Tsuyoshi UdagawaGraduate School of Pharmaceutical Sciences, Tohoku University, Sendai, 980-8578, Japan.
Sihan LiGraduate School of Pharmaceutical Sciences, Tohoku University, Sendai, 980-8578, Japan.
Yasushi SaekiLaboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku, Tokyo, 156-8506, Japan.
Tohru YoshihisaGraduate School of Life Science, University of Hyogo, Hyogo, 678-1297, Japan.
Keiji TanakaLaboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku, Tokyo, 156-8506, Japan.
Nicholas T IngoliaDepartment of Molecular and Cell Biology, University of California, Berkeley, CA94720, USA.
Toshifumi InadaGraduate School of Pharmaceutical Sciences, Tohoku University, Sendai, 980-8578, Japan. toshifumi.inada.a3@tohoku.ac.jp.
Tohoku University · JPTokyo Metropolitan Institute of Medical Science · JPRIKEN · JPUniversity of California, Berkeley · USUniversity of Hyogo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

eIF2α phosphorylation-mediated translational regulation is crucial for global translation repression by various stresses, including the unfolded protein response (UPR). However, translational control during UPR has not been demonstrated in yeast. This study investigated ribosome ubiquitination-mediated translational controls during UPR. Tunicamycin-induced ER stress enhanced the levels of ubiquitination of the ribosomal proteins uS10, uS3 and eS7. Not4-mediated monoubiquitination of eS7A was required for resistance to tunicamycin, whereas E3 ligase Hel2-mediated ubiquitination of uS10 was not. Ribosome profiling showed that the monoubiquitination of eS7A was crucial for translational regulation, including the upregulation of the spliced form of HAC1 (HAC1i) mRNA and the downregulation of Histidine triad NucleoTide-binding 1 (HNT1) mRNA. Downregulation of the deubiquitinating enzyme complex Upb3-Bre5 increased the levels of ubiquitinated eS7A during UPR in an Ire1-independent manner. These findings suggest that the monoubiquitination of ribosomal protein eS7A plays a crucial role in translational controls during the ER stress response in yeast.

Indexed as

Endoplasmic Reticulum StressBasic-Leucine Zipper Transcription FactorsEndopeptidasesGene Expression Regulation, FungalHydrolasesProtein BiosynthesisRepressor ProteinsRibosomal ProteinsRibosomesRNA, FungalRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinationUbiquitin-Protein LigasesUnfolded Protein ResponseBasic-Leucine Zipper Transcription FactorsBre5 protein, S cerevisiaeEndopeptidasesHAC1 protein, S cerevisiaehistidine triad proteinHydrolasesMOT2 protein, S cerevisiaeRepressor ProteinsRibosomal Proteinsribosomal protein S7RNA, FungalRNA, MessengerSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligases

Identifiers

PMID33184379
PMCPMC7661504
OpenAlexW3100366281

What OpenQuestion holds

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LicenceCC BY
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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.