Evidence map›Paper›PMID 27630263›Full record

ArticleMolecular biology of the cell2016

A novel role for yeast casein kinases in glucose sensing and signaling.

Chris Snowdon, Mark Johnston

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed, 1 pooled it
2.1field-weighted citation impact, top 13% 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

27 citing papers in PubMed, 1 synthesis or guideline pooled it, 38 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Sugar-sensing swodkoreceptors and swodkocrine signaling.Animal models and experimental medicine · 2025
    Article
  5. Review
  6. Article
  7. High Glucose Is a Stimulation Signal of the Salt-Tolerant YeastJournal of fungi (Basel, Switzerland) · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Stage-Specific Genetic Interaction betweenInternational journal of molecular sciences · 2022
    Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Alternative Splicing and Cleavage of GLUT8.Molecular and cellular biology · 2020
    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

2 authors at 2 institutions in 1 country.

Chris SnowdonDepartment of Biochemistry and Molecular Genetics, University of Colorado School of Medicine, Aurora, CO 80045.
Mark JohnstonDepartment of Biochemistry and Molecular Genetics, University of Colorado School of Medicine, Aurora, CO 80045 mark.johnston@ucdenver.edu.
Cornell University · USUniversity of Colorado Denver · US

Funding

GLUCOSE SENSING AND SIGNALLING IN YEASTR01GM032540 · NIGMS · WASHINGTON UNIVERSITY · PI JOHNSTON, HENRY MARK · 1985 to 2017
$5.7M
NIGMS NIH HHS R01 GM032540
6 · The paper itself

Abstract

Yeasts have sophisticated signaling pathways for sensing glucose, their preferred carbon source, to regulate its uptake and metabolism. One of these is the sensor/receptor-repressor (SRR) pathway, which detects extracellular glucose and transmits an intracellular signal that induces expression of HXT genes. The yeast casein kinases (Ycks) are key players in this pathway. Our model of the SRR pathway had the Ycks functioning downstream of the glucose sensors, transmitting the signal from the sensors to the Mth1 and Std1 corepressors that are required for repression of HXT gene expression. However, we found that overexpression of Yck1 fails to restore glucose signaling in a glucose sensor mutant. Conversely, overexpression of a glucose sensor suppresses the signaling defect of a yck mutant. These results suggest that the Ycks act upstream or at the level of the glucose sensors. Indeed, we found that the glucose sensor Rgt2 is phosphorylated on Yck consensus sites in its C-terminal tail in a Yck-dependent manner and that this phosphorylation is required for corepressor binding and ultimately HXT expression. This leads to a revised model of the SRR pathway in which the Ycks prime a site on the cytoplasmic tails of the glucose sensors to promote binding of the corepressors.

Indexed as

Adaptor Proteins, Signal TransducingCasein Kinase ICasein KinasesDNA-Binding ProteinsGene Expression Regulation, FungalGlucoseGlucose Transport Proteins, FacilitativeIntracellular Signaling Peptides and ProteinsMembrane ProteinsMonosaccharide Transport ProteinsPhosphorylationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionTranscription FactorsAdaptor Proteins, Signal TransducingCasein Kinase ICasein KinasesDNA-Binding ProteinsGlucoseGlucose Transport Proteins, FacilitativeIntracellular Signaling Peptides and ProteinsMembrane ProteinsMonosaccharide Transport ProteinsMTH1 protein, S cerevisiaeRGT2 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSTD1 protein, S cerevisiaeTranscription Factors

Identifiers

PMID27630263
PMCPMC5170868
OpenAlexW2519870106

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.