Evidence map›Paper›PMID 29038496›Full record

ArticleNature communications2017

The Hsp70 homolog Ssb affects ribosome biogenesis via the TORC1-Sch9 signaling pathway.

Kaivalya Mudholkar, Edith Fitzke, Claudia Prinz, Matthias P Mayer, Sabine Rospert

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

12 citing papers in PubMed, 19 citations in OpenAlex.

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  6. The Adaptation ofJournal of fungi (Basel, Switzerland) · 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

5 authors at 2 institutions in 1 country.

Kaivalya MudholkarInstitute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, D-79104, Freiburg, Germany.
Edith FitzkeInstitute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, D-79104, Freiburg, Germany.
Claudia PrinzInstitute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, D-79104, Freiburg, Germany.
Matthias P MayerCenter for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH-Alliance, D-69120, Heidelberg, Germany.ORCID http://orcid.org/0000-0002-7859-3112
Sabine RospertInstitute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg, D-79104, Freiburg, Germany. sabine.rospert@biochemie.uni-freiburg.de.ORCID http://orcid.org/0000-0002-3089-9614
University of Freiburg · DEHeidelberg University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Hsp70 Ssb serves a dual role in de novo protein folding and ribosome biogenesis; however, the mechanism by which Ssb affects ribosome production is unclear. Here we establish that Ssb is causally linked to the regulation of ribosome biogenesis via the TORC1-Sch9 signaling pathway. Ssb is bound to Sch9 posttranslationally and required for the TORC1-dependent phosphorylation of Sch9 at T737. Also, Sch9 lacking phosphorylation at T737 displays significantly reduced kinase activity with respect to targets involved in the regulation of ribosome biogenesis. The absence of either Ssb or Sch9 causes enhanced ribosome aggregation. Particularly with respect to proper assembly of the small ribosomal subunit, SSB and SCH9 display strong positive genetic interaction. In combination, the data indicate that Ssb promotes ribosome biogenesis not only via cotranslational protein folding, but also posttranslationally via interaction with natively folded Sch9, facilitating access of the upstream kinase TORC1 to Sch9-T737.The yeast Hsp70 homolog Ssb is a chaperone that binds translating ribosomes where it is thought to function primarily by promoting nascent peptide folding. Here the authors find that the ribosome biogenesis defect associated with the loss of Ssb is attributable to a specific disruption in TORC1 signaling rather than defects in ribosomal protein folding.

Indexed as

Adenosine TriphosphatasesDNA-Binding ProteinsHeat-Shock ProteinsHSP70 Heat-Shock ProteinsImmunoblottingMutationPhosphorylationProtein BindingProtein BiosynthesisProtein FoldingProtein Serine-Threonine KinasesRibosomal ProteinsRibosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionAdenosine TriphosphatasesDNA-Binding ProteinsHeat-Shock ProteinsHSF1 protein, S cerevisiaeHSP70 Heat-Shock ProteinsProtein Serine-Threonine KinasesRibosomal ProteinsSaccharomyces cerevisiae ProteinsSCH9 protein, S cerevisiaeSSB1 protein, S cerevisiaeSSB2 protein, S cerevisiaeTORC1 protein complex, S cerevisiaeTranscription Factors

Identifiers

PMID29038496
PMCPMC5643326
OpenAlexW2762551856

What OpenQuestion holds

Textmetadata
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.