Evidence map›Paper›PMID 23297408›Full record

ArticleThe Journal of biological chemistry2013

SUMOylation of pancreatic glucokinase regulates its cellular stability and activity.

Ingvild Aukrust, Lise Bjørkhaug, Maria Negahdar, Janne Molnes, Bente B Johansson, Yvonne Müller, Wilhelm Haas, Steven P Gygi, Oddmund Søvik, Torgeir Flatmark and 2 more

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 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.5field-weighted citation impact, top 8% 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

23 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Review
  3. Regulation of insulin secretion by the post-translational modifications.Frontiers in cell and developmental biology · 2023
    Review
  4. Article
  5. Review
  6. Article
  7. Comprehensive characterization of amino acid positions in protein structures reveals molecular effect of missense variants.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Selenolysine: A New Tool for Traceless Isopeptide Bond Formation.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020
    Article
  9. Molecular and cellular regulation of human glucokinase.Archives of biochemistry and biophysics · 2019
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Liver glucose metabolism in humans.Bioscience reports · 2016
    Review
  17. Article
  18. Article
  19. SUMOylation protects against IL-1β-induced apoptosis in INS-1 832/13 cells and human islets.American journal of physiology. Endocrinology and metabolism · 2014
    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

12 authors at 3 institutions in 2 countries.

Ingvild AukrustKG Jebsen Center for Diabetes Research, Department of Clinical Medicine, N-5020 Bergen, Norway.
Lise Bjørkhaug
Maria Negahdar
Janne Molnes
Bente B Johansson
Yvonne Müller
Wilhelm Haas
Steven P Gygi
Oddmund Søvik
Torgeir Flatmark
Rohit N Kulkarni
Pål R Njølstad
Harvard University · USHaukeland University Hospital · NOUniversity of Bergen · NO

Funding

New Sample Multiplexing Technologies to Identify Chemical Probes and Illuminate Ubiquitin BiologyR01GM067945 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI GYGI, STEVEN P · 2003 to 2024
$10.5M
Role of IGF-1 and Insulin Receptors Beta-Cell SurvivalR01DK067536 · NIDDK · JOSLIN DIABETES CENTER · PI ROHIT N. KULKARNI · 2004 to 2026
$8.0M
NIDDK NIH HHS R01 DK067536NIGMS NIH HHS R01 GM067945
6 · The paper itself

Abstract

Glucokinase is the predominant hexokinase expressed in hepatocytes and pancreatic β-cells, with a pivotal role in regulating glucose-stimulated insulin secretion, illustrated by glucokinase gene mutations causing monogenic diabetes and congenital hyperinsulinemic hypoglycemia. A complex tissue-specific network of mechanisms regulates this enzyme, and a major unanswered question in glucokinase biology is how post-translational modifications control the function of the enzyme. Here, we show that the pancreatic isoform of human glucokinase is SUMOylated in vitro, using recombinant enzymes, and in insulin-secreting model cells. Three N-terminal lysines unique for the pancreatic isoform (Lys-12/Lys-13 and/or Lys-15) may represent one SUMOylation site, with an additional site (Lys-346) common for the pancreatic and the liver isoform. SUMO-1 and E2 overexpression stabilized preferentially the wild-type human pancreatic enzyme in MIN6 β-cells, and SUMOylation increased the catalytic activity of recombinant human glucokinase in vitro and also of glucokinase in target cells. Small ubiquitin-like modifier conjugation represents a novel form of post-translational modification of the enzyme, and it may have an important regulatory function in pancreatic β-cells.

Indexed as

Gene Expression Regulation, EnzymologicSumoylationAnimalsCarbohydratesCatalysisElectrophoresis, Gel, Two-DimensionalGlucokinaseInsulin-Secreting CellsKineticsLiverMass SpectrometryMiceMutationPancreasProtein IsoformsProtein Processing, Post-TranslationalCarbohydratesGlucokinaseProtein IsoformsRecombinant Proteins

Identifiers

PMID23297408
PMCPMC3581398
OpenAlexW2091680105

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.