Evidence map›Paper›PMID 26865637›Full record

ArticleThe Journal of biological chemistry2016

Hexokinase 2 Is an Intracellular Glucose Sensor of Yeast Cells That Maintains the Structure and Activity of Mig1 Protein Repressor Complex.

Montserrat Vega, Alberto Riera, Alejandra Fernández-Cid, Pilar Herrero, Fernando Moreno

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
5.7field-weighted citation impact, top 4% 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

51 citing papers in PubMed, 91 citations in OpenAlex.

  1. Glucose repression ofbioRxiv : the preprint server for biology · 2026
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  3. Review
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  8. Sugar-sensing swodkoreceptors and swodkocrine signaling.Animal models and experimental medicine · 2025
    Article
  9. Article
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  12. Article
  13. Review
  14. Article
  15. Article
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  17. Review
  18. Regulation of Fungal Morphogenesis and Pathogenicity ofJournal of fungi (Basel, Switzerland) · 2023
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Montserrat VegaFrom the Department of Biochemistry and Molecular Biology, University of Oviedo, 33006-Oviedo, Spain.
Alberto RieraFrom the Department of Biochemistry and Molecular Biology, University of Oviedo, 33006-Oviedo, Spain.
Alejandra Fernández-CidFrom the Department of Biochemistry and Molecular Biology, University of Oviedo, 33006-Oviedo, Spain.
Pilar HerreroFrom the Department of Biochemistry and Molecular Biology, University of Oviedo, 33006-Oviedo, Spain.
Fernando MorenoFrom the Department of Biochemistry and Molecular Biology, University of Oviedo, 33006-Oviedo, Spain fmoreno@uniovi.es.
Universidad de Oviedo · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hexokinase 2 (Hxk2) fromSaccharomyces cerevisiaeis a bi-functional enzyme, being both a catalyst in the cytosol and an important regulator of the glucose repression signal in the nucleus. Despite considerable recent progress, little is known about the regulatory mechanism that controls nuclear Hxk2 association with theSUC2promoter chromatin and how this association is necessary forSUC2gene repression. Our data indicate that in theSUC2promoter context, Hxk2 functions through a variety of structurally unrelated factors, mainly the DNA-binding Mig1 and Mig2 repressors and the regulatory Snf1 and Reg1 factors. Hxk2 sustains the repressor complex architecture maintaining transcriptional repression at theSUC2gene. Using chromatin immunoprecipitation assays, we discovered that the Hxk2 in its open configuration, at low glucose conditions, leaves the repressor complex that induces its dissociation and promotesSUC2gene expression. In high glucose conditions, Hxk2 adopts a close conformation that promotes Hxk2 binding to the Mig1 protein and the reassembly of theSUC2repressor complex. Additional findings highlight the possibility that Hxk2 constitutes an intracellular glucose sensor that operates by changing its conformation in response to cytoplasmic glucose levels that regulate its interaction with Mig1 and thus its recruitment to the repressor complex of theSUC2promoter. Thus, our data indicate that Hxk2 is more intimately involved in gene regulation than previously thought.

Indexed as

beta-FructofuranosidaseGlucoseHexokinaseMultiprotein ComplexesProtein BindingProtein Phosphatase 1Protein Serine-Threonine KinasesRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteinsbeta-FructofuranosidaseGlucoseHexokinaseHXK2 protein, S cerevisiaeMIG1 protein, S cerevisiaeMultiprotein ComplexesProtein Phosphatase 1Protein Serine-Threonine KinasesREG1 protein, S cerevisiaeRepressor ProteinsSaccharomyces cerevisiae ProteinsSNF1-related protein kinasesSUC2 protein, S cerevisiaegene expressionglucoseglucose signalinghexokinaserepressor proteinSaccharomyces cerevisiae

Identifiers

PMID26865637
PMCPMC4817161
OpenAlexW2255671650

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.