Evidence map›Paper›PMID 17586499›Full record

ArticleFEBS letters2007

Biochemical evidence for glucose-independent induction of HXT expression in Saccharomyces cerevisiae.

Satish Pasula, David Jouandot, Jeong-Ho Kim

Open access · greenAbstract read
In one paragraph

Article in FEBS letters, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

25 citing papers in PubMed, 37 citations in OpenAlex.

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  14. The glucose signaling network in yeast.Biochimica et biophysica acta · 2013
    Review
  15. SUMOylation regulates the SNF1 protein kinase.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  16. Review
  17. 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

3 authors at 1 institution in 1 country.

Satish PasulaMississippi Functional Genomics Network, Department of Biological Sciences, The University of Southern Mississippi, Hattiesburg, MS 39406, USA.
David Jouandot
Jeong-Ho Kim
University of Southern Mississippi · US

Funding

TOUGALOO PROTEOMICSP20RR016476 · NCRR · UNIVERSITY OF SOUTHERN MISSISSIPPI · PI SHEARER, GLEN · 2001 to 2011
$30.4M
NCRR NIH HHS P20 RR016476NCRR NIH HHS RR016476-04
6 · The paper itself

Abstract

The yeast glucose sensors Rgt2 and Snf3 generate a signal in response to glucose that leads to degradation of Mth1 and Std1, thereby relieving repression of Rgt1-repressed genes such as the glucose transporter genes (HXT). Mth1 and Std1 are degraded via the Yck1/2 kinase-SCF(Grr1)-26S proteasome pathway triggered by the glucose sensors. Here, we show that RGT2-1 promotes ubiquitination and subsequent degradation of Mth1 and Std1 regardless of the presence of glucose. Site-specific mutagenesis reveals that the conserved lysine residues of Mth1 and Std1 might serve as attachment sites for ubiquitin, and that the potential casein kinase (Yck1/2) sites of serine phosphorylation might control their ubiquitination. Finally, we show that active Snf1 protein kinase in high glucose prevents degradation of Mth1 and Std1.

Indexed as

Adaptor Proteins, Signal TransducingBinding SitesCasein Kinase IEnzyme ActivationF-Box ProteinsGene Expression Regulation, FungalGlucoseIntracellular Signaling Peptides and ProteinsLysineMembrane ProteinsMonosaccharide Transport ProteinsPhosphorylationProtein IsoformsProtein Processing, Post-TranslationalProtein Serine-Threonine KinasesSaccharomyces cerevisiaeAdaptor Proteins, Signal TransducingCasein Kinase IF-Box ProteinsGlucoseGRR1 protein, S cerevisiaeIntracellular Signaling Peptides and ProteinsLysineMembrane ProteinsMonosaccharide Transport ProteinsMTH1 protein, S cerevisiaeProtein IsoformsProtein Serine-Threonine KinasesRGT2 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSKP Cullin F-Box Protein LigasesSNF1-related protein kinasesSTD1 protein, S cerevisiaeUbiquitinUbiquitin-Protein LigasesYCK1 protein, S cerevisiaeYCK2 protein, S cerevisiae

Identifiers

PMID17586499
PMCPMC2040036
OpenAlexW1977370230

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.