Evidence map›Paper›PMID 29147007›Full record

ArticleExperimental & molecular medicine2017

Modulating cellular balance of Rps3 mono-ubiquitination by both Hel2 E3 ligase and Ubp3 deubiquitinase regulates protein quality control.

Youjin Jung, Hag Dong Kim, Hee Woong Yang, Hye Jin Kim, Chang-Young Jang, Joon Kim

Open access · goldAbstract read
In one paragraph

Article in Experimental & molecular medicine, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

34 citing papers in PubMed, 56 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

6 authors at 2 institutions in 1 country.

Youjin JungLaboratory of Biochemistry, Division of Life Sciences, Korea University, Seoul, Republic of Korea.
Hag Dong KimLaboratory of Biochemistry, Division of Life Sciences, Korea University, Seoul, Republic of Korea.
Hee Woong YangLaboratory of Biochemistry, Division of Life Sciences, Korea University, Seoul, Republic of Korea.
Hye Jin KimLaboratory of Biochemistry, Division of Life Sciences, Korea University, Seoul, Republic of Korea.
Chang-Young JangLaboratory of Cell Biology, Research Center for Cell Fate Control, College of Pharmacy, Sookmyung Women's University, Seoul, Republic of Korea.
Joon KimLaboratory of Biochemistry, Division of Life Sciences, Korea University, Seoul, Republic of Korea.
Korea University · KRSookmyung Women's University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

When a ribosome complex is stalled during the translation elongation process in eukaryotes, the mono-ubiquitination of Rps3 has recently been shown to be critical to ribosome quality control. We have discovered that the regulatory role of Rps3 mono-ubiquitination is controlled by a deubiquitinase. We also showed that an autophagic signal appears to be coupled to the mono-ubiquitination of Rps3p through the entrance of Ubp3p into the autophagosome in yeasts. The mono-ubiquitination of the Rps3 protein is tightly modulated by reciprocal action between the Hel2p E3 ligase and the Ubp3p deubiquitinase in yeasts and the reciprocal action between the RNF123 E3 ligase and the USP10 deubiquitinase in mammalian cells. We also found that the Ubp3p/USP10 deubiquitinases critically modulate Hel2p/RNF123-mediated Rps3p mono-ubiquitination. In addition, we found that Hel2p/RNF123 and Ubp3p/USP10 appeared to be differently localized in the ribosome complex after ultraviolet irradiation. Together, our results support a model in which coordinated ubiquitination and deubiquitination activities can finely balance the level of regulatory Rps3p mono-ubiquitination in ribosome-associated quality control and autophagy processes.

Indexed as

Amino AcidsApoptosisCell SurvivalEndopeptidasesHumansProtein BiosynthesisProtein Processing, Post-TranslationalRibosomal ProteinsRibosomesSaccharomyces cerevisiae ProteinsUbiquitinationUbiquitin-Protein LigasesUbiquitin ThiolesteraseAmino AcidsEndopeptidasesHel2 protein, S cerevisiaeRibosomal Proteinsribosomal protein S3RPS3 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Protein LigasesUbiquitin ThiolesteraseUBP3 protein, S cerevisiae

Identifiers

PMID29147007
PMCPMC5704183
OpenAlexW2769121188

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.