Evidence map›Paper›PMID 29352143›Full record

ArticleScientific reports2018

Ribosomal protein uS7/Rps5 serine-223 in protein kinase-mediated phosphorylation and ribosomal small subunit maturation.

Makoto Tomioka, Mitsugu Shimobayashi, Makoto Kitabatake, Mutsuhito Ohno, Yasunori Kozutsumi, Shogo Oka, Hiromu Takematsu

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.5field-weighted citation impact, top 38% 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

10 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Eukaryotic Ribosomal Protein S5 of the 40S Subunit: Structure and Function.International journal of molecular sciences · 2023
    Review
  5. Article
  6. Review
  7. Regulation of ribosomal protein genes: An ordered anarchy.Wiley interdisciplinary reviews. RNA · 2021
    Review
  8. Observational
  9. Article
  10. Protein Kinases at the Intersection of Translation and Virulence.Frontiers in cellular and infection microbiology · 2019
    Review
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

7 authors at 1 institution in 1 country.

Makoto TomiokaLaboratory of Biological Chemistry, Human Health Sciences, Graduate School of Medicine, Kyoto University, Kyoto, Japan.
Mitsugu ShimobayashiLaboratory of Membrane Biochemistry and Biophysics, Graduate School of Biostudies, Kyoto University, Kyoto, Japan.
Makoto KitabatakeLaboratory of RNA System, Institute for Frontier Life and Medical Sciences, Kyoto University, Kyoto, Japan.
Mutsuhito OhnoLaboratory of RNA System, Institute for Frontier Life and Medical Sciences, Kyoto University, Kyoto, Japan.
Yasunori KozutsumiLaboratory of Membrane Biochemistry and Biophysics, Graduate School of Biostudies, Kyoto University, Kyoto, Japan.
Shogo OkaLaboratory of Biological Chemistry, Human Health Sciences, Graduate School of Medicine, Kyoto University, Kyoto, Japan.
Hiromu TakematsuLaboratory of Biological Chemistry, Human Health Sciences, Graduate School of Medicine, Kyoto University, Kyoto, Japan. htakema@pharm.kyoto-u.ac.jp.
Kyoto University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cellular translation should be precisely controlled in response to extracellular cues. However, knowledge is limited concerning signal transduction-regulated translation. In the present study, phosphorylation was identified in the 40S small subunit ribosomal protein uS7 (Yjr123w/previously called as Rps5) by Ypk1 and Pkc1, AGC family protein kinases in yeast Saccharomyces cerevisiae. Serine residue 223 (Ser223) of uS7 in the conserved C-terminal region was crucial for this phosphorylation event. S223A mutant uS7 caused severe reduction of small ribosomal subunit production, likely due to compromised interaction with Rio2, resulting in both reduced translation and reduced cellular proliferation. Contrary to optimal culture conditions, heat stressed S223A mutant cells exhibited increased heat resistance and induced heat shock proteins. Taken together, an intracellular signal transduction pathway involving Ypk1/Pkc1 seemed to play an important role in ribosome biogenesis and subsequent cellular translation, utilizing uS7 as a substrate.

Indexed as

Protein Processing, Post-TranslationalHeat-Shock ResponseMutationPhosphorylationProtein DomainsProtein Kinase CProtein Serine-Threonine KinasesRibosomal ProteinsRibosome Subunits, SmallSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionPKC1 protein, S cerevisiaeProtein Kinase CProtein Serine-Threonine KinasesRibosomal Proteinsribosomal protein S5Saccharomyces cerevisiae ProteinsYPK1 protein, S cerevisiae

Identifiers

PMID29352143
PMCPMC5775349
OpenAlexW2782908525

What OpenQuestion holds

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LicenceCC BY
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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.