Evidence map›Paper›PMID 23066030›Full record

ArticleThe Journal of biological chemistry2012

Phosphorylation of yeast hexokinase 2 regulates its nucleocytoplasmic shuttling.

Paula Fernández-García, Rafael Peláez, Pilar Herrero, Fernando Moreno

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
5.6field-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

43 citing papers in PubMed, 81 citations in OpenAlex.

  1. Glucose repression ofbioRxiv : the preprint server for biology · 2026
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. When Phosphatases Go Mad: The Molecular Basis for Toxicity of Yeast Ppz1.International journal of molecular sciences · 2022
    Review
  11. D-Xylose Sensing inInternational journal of molecular sciences · 2021
    Review
  12. Article
  13. Microorganisms · 2021
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Moonlighting Proteins: The Case of the Hexokinases.Frontiers in molecular biosciences · 2021
    Review
  19. Article
  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

4 authors at 1 institution in 1 country.

Paula Fernández-GarcíaDepartment of Biochemistry and Molecular Biology, University of Oviedo, 33006 Oviedo, Spain.
Rafael Peláez
Pilar Herrero
Fernando Moreno
Universidad de Oviedo · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nucleocytoplasmic shuttling of Hxk2 induced by glucose levels has been reported recently. Here we present evidence that indicates that Hxk2 nucleocytoplasmic traffic is regulated by phosphorylation and dephosphorylation at serine 14. Moreover, we identified the protein kinase Snf1 and the protein phosphatase Glc7-Reg1 as novel regulatory partners for the nucleocytoplasmic shuttling of Hxk2. Functional studies revealed that, in contrast to the wild-type protein, the dephosphorylation-mimicking mutant of Hxk2 retains its nuclear localization in low glucose conditions, and the phosphomimetic mutant of Hxk2 retains its cytoplasmic localization in high glucose conditions. Interaction experiments of Hxk2 with Kap60 and Xpo1 indicated that nuclear import of the S14D mutant of Hxk2 is severely decreased but that the export is significantly enhanced. Conversely, nuclear import of the S14A mutant of Hxk2 was significantly enhanced, although the export was severely decreased. The interaction of Hxk2 with Kap60 and Xpo1 was found to occur in the dephosphorylated and phosphorylated states of the protein, respectively. In addition, we found that Hxk2 is a substrate for Snf1. Mutational analysis indicated that serine 14 is a major in vitro and in vivo phosphorylation site for Snf1. We also provide evidence that dephosphorylation of Hxk2 at serine 14 is a protein phosphatase Glc7-Reg1-dependent process. Taken together, this study establishes a functional link between Hxk2, Reg1, and Snf1 signaling, which involves the regulation of Hxk2 nucleocytoplasmic shuttling by phosphorylation-dephosphorylation of serine 14.

Indexed as

Active Transport, Cell NucleusAmino Acid SubstitutionCell NucleusCytoplasmExportin 1 ProteinHexokinaseKaryopherinsMutation, MissensePhosphorylationProtein Phosphatase 1Protein Serine-Threonine KinasesReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionExportin 1 ProteinGLC7 protein, S cerevisiaeHexokinaseHXK2 protein, S cerevisiaeKaryopherinsProtein Phosphatase 1Protein Serine-Threonine KinasesReceptors, Cytoplasmic and NuclearREG1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSNF1-related protein kinases

Identifiers

PMID23066030
PMCPMC3516761
OpenAlexW2025505237

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.