Evidence map›Paper›PMID 24187134›Full record

ArticleThe Journal of biological chemistry2013

Identification of the ubiquitin-like domain of midnolin as a new glucokinase interaction partner.

Anke Hofmeister-Brix, Katrin Kollmann, Sara Langer, Julia Schultz, Sigurd Lenzen, Simone Baltrusch

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.0field-weighted citation impact, top 14% 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, 41 citations in OpenAlex.

  1. Article
  2. Targeted degradation of c-Myc through the midnolin-proteasome pathway.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. Viable mutations of mouse midnolin suppress B cell malignancies.The Journal of experimental medicine · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Midnolin is a confirmed genetic risk factor for Parkinson's disease.Annals of clinical and translational neurology · 2019
    Article
  16. Article
  17. Article
  18. Molecular and cellular regulation of human glucokinase.Archives of biochemistry and biophysics · 2019
    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

6 authors at 2 institutions in 1 country.

Anke Hofmeister-BrixFrom the Institute of Clinical Biochemistry, Hannover Medical School, 30625 Hannover, Germany and.
Katrin Kollmann
Sara Langer
Julia Schultz
Sigurd Lenzen
Simone Baltrusch
Medizinische Hochschule Hannover · DEUniversity of Rostock · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glucokinase acts as a glucose sensor in pancreatic beta cells. Its posttranslational regulation is important but not yet fully understood. Therefore, a pancreatic islet yeast two-hybrid library was produced and searched for glucokinase-binding proteins. A protein sequence containing a full-length ubiquitin-like domain was identified to interact with glucokinase. Mammalian two-hybrid and fluorescence resonance energy transfer analyses confirmed the interaction between glucokinase and the ubiquitin-like domain in insulin-secreting MIN6 cells and revealed the highest binding affinity at low glucose. Overexpression of parkin, an ubiquitin E3 ligase exhibiting an ubiquitin-like domain with high homology to the identified, diminished insulin secretion in MIN6 cells but had only some effect on glucokinase activity. Overexpression of the elucidated ubiquitin-like domain or midnolin, containing exactly this ubiquitin-like domain, significantly reduced both intrinsic glucokinase activity and glucose-induced insulin secretion. Midnolin has been to date classified as a nucleolar protein regulating mouse development. However, we could not confirm localization of midnolin in nucleoli. Fluorescence microscopy analyses revealed localization of midnolin in nucleus and cytoplasm and co-localization with glucokinase in pancreatic beta cells. In addition we could show that midnolin gene expression in pancreatic islets is up-regulated at low glucose and that the midnolin protein is highly expressed in pancreatic beta cells and also in liver, muscle, and brain of the adult mouse and cell lines of human and rat origin. Thus, the results of our study suggest that midnolin plays a role in cellular signaling of adult tissues and regulates glucokinase enzyme activity in pancreatic beta cells.

Indexed as

Amino Acid SequenceAnimalsCell LineCell SurvivalGene Expression Regulation, EnzymologicGlucokinaseGlucoseHumansInsulinInsulin-Secreting CellsInsulin SecretionMaleMiceModels, MolecularMolecular Sequence DataNuclear ProteinsGlucokinaseGlucoseInsulinmidnolinNuclear Proteinsparkin proteinPeptide FragmentsUbiquitinUbiquitin-Protein LigasesFluorescence Resonance Energy Transfer (FRET)GlucokinaseInsulin SecretionInsulin SynthesisMidnolinPancreatic IsletsParkinTwo-hybrid SystemUbiquitinUbiquitin-like Domain

Identifiers

PMID24187134
PMCPMC3861633
OpenAlexW2002588250

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.