Evidence map›Paper›PMID 22333918›Full record

ArticleThe EMBO journal2012

PP4 dephosphorylates Maf1 to couple multiple stress conditions to RNA polymerase III repression.

Andrew J Oler, Bradley R Cairns

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Regulation of Eukaryotic RNAPs Activities by Phosphorylation.Frontiers in molecular biosciences · 2021
    Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Glycolytic flux inThe Biochemical journal · 2019
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
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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

2 authors at 2 institutions in 1 country.

Andrew J OlerHHMI, Department of Oncological Sciences, Huntsman Cancer Institute, University of Utah School of Medicine, Salt Lake City, UT, USA.
Bradley R Cairns
Huntsman Cancer Institute · USUniversity of Utah · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Maf1 is the 'master' repressor of RNA polymerase III (Pol III) transcription in yeast, and is conserved in eukaryotes. Maf1 is a phospho-integrator, with unfavourable growth conditions leading to rapid Maf1 dephosphorylation, nuclear accumulation, binding to RNA Pol III at Pol III genes and transcriptional repression. Here, we establish the protein phosphatase 4 (PP4) complex as the main Maf1 phosphatase, and define the involved catalytic (Pph3), scaffold (Psy2) and regulatory subunits (Rrd1, Tip41), as well as uninvolved subunits (Psy4, Rrd2). Multiple approaches support a central role for PP4 in Maf1 dephosphorylation, Maf1 nuclear localization and the rapid repression of Pol III in the nucleus. PP4 action is likely direct, as a portion of PP4 co-precipitates with Maf1, and purified PP4 dephosphorylates Maf1 in vitro. Furthermore, Pph3 mediates (either largely or fully) rapid Maf1 dephosphorylation in response to diverse stresses, suggesting PP4 plays a key role in the integration of cell nutrition and stress conditions by Maf1 to enable Pol III regulation.

Indexed as

Cell NucleusIntracellular Signaling Peptides and ProteinsNuclear ProteinsPeptidylprolyl IsomerasePhosphoprotein PhosphatasesPhosphorylationRecombinant Fusion ProteinsRNA Polymerase IIISaccharomyces cerevisiae ProteinsTranscription FactorsTranscription, GeneticIntracellular Signaling Peptides and ProteinsMAF1 protein, S cerevisiaeNuclear ProteinsPeptidylprolyl IsomerasePhosphoprotein PhosphatasesPPH3 protein, S cerevisiaeprotein phosphatase 4Psy2 protein, S cerevisiaePsy4 protein, S cerevisiaeRecombinant Fusion ProteinsRNA Polymerase IIIRRD1 protein, S cerevisiaeRRD2 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTIP41 protein, S cerevisiaeTranscription Factors

Identifiers

PMID22333918
PMCPMC3321174
OpenAlexW2138209473

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.