Evidence map›Paper›PMID 25593311›Full record

ArticleThe Journal of biological chemistry2015

Protein kinase Ymr291w/Tda1 is essential for glucose signaling in saccharomyces cerevisiae on the level of hexokinase isoenzyme ScHxk2 phosphorylation*.

Sonja Kaps, Karina Kettner, Rebekka Migotti, Tamara Kanashova, Udo Krause, Gerhard Rödel, Gunnar Dittmar, Thomas M Kriegel

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

18 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Microorganisms · 2021
    Article
  11. Moonlighting Proteins: The Case of the Hexokinases.Frontiers in molecular biosciences · 2021
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. The Expanding Landscape of Moonlighting Proteins in Yeasts.Microbiology and molecular biology reviews : MMBR · 2016
    Review
  17. Article
  18. 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

8 authors at 2 institutions in 1 country.

Sonja KapsFrom the Institute of Physiological Chemistry, Faculty of Medicine Carl Gustav Carus, Technische Universität Dresden, 01307 Dresden.
Karina KettnerFrom the Institute of Physiological Chemistry, Faculty of Medicine Carl Gustav Carus, Technische Universität Dresden, 01307 Dresden, Karina.Kettner@tu-dresden.de.
Rebekka Migottithe Mass Spectrometry Platform, Max Delbrück Center for Molecular Medicine, 13125 Berlin, and.
Tamara Kanashovathe Mass Spectrometry Platform, Max Delbrück Center for Molecular Medicine, 13125 Berlin, and.
Udo Krausethe Institute of Genetics, Technische Universität Dresden, 01062 Dresden, Germany.
Gerhard Rödelthe Institute of Genetics, Technische Universität Dresden, 01062 Dresden, Germany.
Gunnar Dittmarthe Mass Spectrometry Platform, Max Delbrück Center for Molecular Medicine, 13125 Berlin, and.
Thomas M KriegelFrom the Institute of Physiological Chemistry, Faculty of Medicine Carl Gustav Carus, Technische Universität Dresden, 01307 Dresden.
Max Delbrück Center · DETU Dresden · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The enzyme ScHxk2 of Saccharomyces cerevisiae is a dual-function hexokinase that besides its catalytic role in glycolysis is involved in the transcriptional regulation of glucose-repressible genes. Relief from glucose repression is accompanied by the phosphorylation of the nuclear fraction of ScHxk2 at serine 15 and the translocation of the phosphoenzyme into the cytosol. Different studies suggest different serine/threonine protein kinases, Ymr291w/Tda1 or Snf1, to accomplish ScHxk2-S15 phosphorylation. The current paper provides evidence that Ymr291w/Tda1 is essential for that modification, whereas protein kinases Ydr477w/Snf1, Ynl307c/Mck1, Yfr014c/Cmk1, and Ykl126w/Ypk1, which are co-purified during Ymr291w/Tda1 tandem affinity purification, as well as protein kinase PKA and PKB homolog Sch9 are dispensable. Taking into account the detection of a significantly higher amount of the Ymr291w/Tda1 protein in cells grown in low-glucose media as compared with a high-glucose environment, Ymr291w/Tda1 is likely to contribute to glucose signaling in S. cerevisiae on the level of ScHxk2-S15 phosphorylation in a situation of limited external glucose availability. The evolutionary conservation of amino acid residue serine 15 in yeast hexokinases and its phosphorylation is illustrated by the finding that YMR291W/TDA1 of S. cerevisiae and the homologous KLLA0A09713 gene of Kluyveromyces lactis allow for cross-complementation of the respective protein kinase single-gene deletion strains.

Indexed as

GlycolysisAmino Acid SequenceGene Expression Regulation, FungalGlucoseHexokinaseIsoenzymesKluyveromycesPhosphorylationProtein Serine-Threonine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSerineSignal TransductionSubstrate SpecificityGlucoseHexokinaseHXK2 protein, S cerevisiaeIsoenzymesProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsSerineHexokinaseKluyveromyces lactisPhosphorylationProtein Kinase A (PKA)Saccharomyces cerevisiaeSch9ScHxk2SignalingSnf1Ymr291w/Tda1

Identifiers

PMID25593311
PMCPMC4358262
OpenAlexW2087889644

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.