Evidence map›Paper›PMID 11854400›Full record

ArticleMolecular biology of the cell2002

The eukaryotic two-component histidine kinase Sln1p regulates OCH1 via the transcription factor, Skn7p.

Sheng Li, Susan Dean, Zhijian Li, Joe Horecka, Robert J Deschenes, Jan S Fassler

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

54 citing papers in PubMed, 95 citations in OpenAlex.

  1. Review
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  3. Review
  4. Review
  5. Article
  6. Article
  7. Oxidative stress response pathways in fungi.Cellular and molecular life sciences : CMLS · 2022
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. The yeasts phosphorelay systems: a comparative view.World journal of microbiology & biotechnology · 2017
    Review
  15. Article
  16. Article
  17. Article
  18. Article
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  20. Article
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 2 countries.

Sheng LiDepartment of Biological Sciences, University of Iowa, University of Iowa, Iowa City, Iowa 52242, USA.
Susan Dean
Zhijian Li
Joe Horecka
Robert J Deschenes
Jan S Fassler
University of Iowa · USNational Institute of Advanced Industrial Science and Technology · JP

Funding

SIGNAL TRANSDUCTION BY A YEAST TWO COMPONENT REGULATORR01GM056719 · NIGMS · UNIVERSITY OF IOWA · PI FASSLER, JAN S. · 1998 to 2005
$1.7M
Regulation of eukaryotic histidine kinasesR01GM068746 · NIGMS · UNIVERSITY OF IOWA · PI DESCHENES, ROBERT J · 2003 to 2006
$1.1M
NIGMS NIH HHS GM56719NIGMS NIH HHS R01 GM056719NIGMS NIH HHS R01 GM068746
6 · The paper itself

Abstract

The yeast "two-component" osmotic stress phosphorelay consists of the histidine kinase, Sln1p, the phosphorelay intermediate, Ypd1p and two response regulators, Ssk1p and Skn7p, whose activities are regulated by phosphorylation of a conserved aspartyl residue in the receiver domain. Dephospho-Ssk1p leads to activation of the hyper-osmotic response (HOG) pathway, whereas phospho-Skn7p presumably leads to activation of hypo-osmotic response genes. The multifunctional Skn7 protein is important in oxidative as well as osmotic stress; however, the Skn7p receiver domain aspartate that is the phosphoacceptor in the SLN1 pathway is dispensable for oxidative stress. Like many well-characterized bacterial response regulators, Skn7p is a transcription factor. In this report we investigate the role of Skn7p in osmotic response gene activation. Our studies reveal that the Skn7p HSF-like DNA binding domain interacts with a cis-acting element identified upstream of OCH1 that is distinct from the previously defined HSE-like Skn7p binding site. Our data support a model in which Skn7p receiver domain phosphorylation affects transcriptional activation rather than DNA binding to this class of DNA binding site.

Indexed as

MannosyltransferasesProtein KinasesSaccharomyces cerevisiae ProteinsAspartic AcidBinding SitesCell WallDNA-Binding ProteinsFungal ProteinsGene Expression Regulation, FungalIntracellular Signaling Peptides and ProteinsMembrane GlycoproteinsPromoter Regions, GeneticResponse ElementsSaccharomyces cerevisiaeSequence Analysis, DNASignal TransductionAspartic AcidDNA-Binding ProteinsFungal ProteinsIntracellular Signaling Peptides and ProteinsMannosyltransferasesMembrane GlycoproteinsOCH1 protein, S cerevisiaeProtein KinasesSaccharomyces cerevisiae ProteinsSKN7 protein, S cerevisiaeSLN1 protein, S cerevisiaeTranscription Factors

Identifiers

PMID11854400
PMCPMC65637
OpenAlexW2154292068

What OpenQuestion holds

Textmetadata
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.