Evidence map›Paper›PMID 20386698›Full record

ArticlePloS one2010

Phosphorylation of Not4p functions parallel to BUR2 to regulate resistance to cellular stresses in Saccharomyces cerevisiae.

Nga-Chi Lau, Klaas W Mulder, Arjan B Brenkman, Shabaz Mohammed, Niels J F van den Broek, Albert J R Heck, H Th Marc Timmers

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.5field-weighted citation impact, top 34% 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

13 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
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  4. Review
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  7. Article
  8. The complexity of miRNA-mediated repression.Cell death and differentiation · 2015
    Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Ccr4-Not complex: the control freak of eukaryotic cells.Critical reviews in biochemistry and molecular biology
    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 3 institutions in 1 country.

Nga-Chi LauDepartment of Physiological Chemistry, University Medical Center Utrecht, Utrecht, The Netherlands.
Klaas W Mulder
Arjan B Brenkman
Shabaz Mohammed
Niels J F van den Broek
Albert J R Heck
H Th Marc Timmers
University Medical Center Utrecht · NLNetherlands Metabolomics Centre · NLUtrecht University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe evolutionarily conserved Ccr4-Not and Bur1/2 kinase complexes are functionally related in Saccharomyces cerevisiae. In this study, we further explore the relationship between the subunits Not4p and Bur2p. METHODOLOGY/PRINCIPAL

findingsFirst, we investigated the presence of post-translational modifications on the Ccr4-Not complex. Using mass spectrometry analyses we identified several SP/TP phosphorylation sites on its Not4p, Not1p and Caf1p subunits. Secondly, the influence of Not4p phosphorylation on global H3K4 tri-methylation status was examined by immunoblotting. This histone mark is severely diminished in the absence of Not4p or of Bur2p, but did not require the five identified Not4p phosphorylation sites. Thirdly, we found that Not4p phosphorylation is not affected by the kinase-defective bur1-23 mutant. Finally, phenotypic analyses of the Not4p phosphomutant (not4S/T5A) and bur2Delta strains showed overlapping sensitivities to drugs that abolish cellular stress responses. The double-mutant not4S/T5A and bur2Delta strain even revealed enhanced phenotypes, indicating that phosphorylation of Not4p and BUR2 are active in parallel pathways for drug tolerance.

conclusionsNot4p is a phospho-protein with five identified phosphorylation sites that are likely targets of a cyclin-dependent kinase(s) other than the Bur1/2p complex. Not4p phosphorylation on the five Not4 S/T sites is not required for global H3K4 tri-methylation. In contrast, Not4p phosphorylation is involved in tolerance to cellular stresses and acts in pathways parallel to BUR2 to affect stress responses in Saccharomyces cerevisiae.

Indexed as

Stress, PhysiologicalCyclinsHistonesMethylationMultiprotein ComplexesMutationPhosphorylationRepressor ProteinsSaccharomyces cerevisiae ProteinsUbiquitin-Protein LigasesBur2 protein, S cerevisiaeCyclinsHistonesMOT2 protein, S cerevisiaeMultiprotein ComplexesRepressor ProteinsSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligases

Identifiers

PMID20386698
PMCPMC2851644
OpenAlexW2029861927

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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.