Evidence map›Paper›PMID 23946484›Full record

ArticleThe Journal of biological chemistry2013

O-linked N-acetylglucosamine cycling regulates mitotic spindle organization.

Ee Phie Tan, Sarah Caro, Anish Potnis, Christopher Lanza, Chad Slawson

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 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.5field-weighted citation impact, top 21% 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

25 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Regulation of Liver Regeneration by Hepatocyte O-GlcNAcylation in Mice.Cellular and molecular gastroenterology and hepatology · 2022
    Article
  6. Phospho-regulation of mitotic spindle assembly.Cytoskeleton (Hoboken, N.J.) · 2020
    Review
  7. The Journal of biological chemistry · 2020
    Article
  8. Centrosomes: Til O-GlcNAc Do Us Apart.Frontiers in endocrinology · 2020
    Review
  9. Review
  10. Article
  11. O-GlcNAc: a novel regulator of immunometabolism.Journal of bioenergetics and biomembranes · 2018
    Review
  12. Molecules (Basel, Switzerland) · 2018
    Article
  13. Article
  14. Review
  15. SustainedThe Journal of biological chemistry · 2017
    Article
  16. Article
  17. The sweet side of the cell cycle.Biochemical Society transactions · 2017
    Review
  18. O-GlcNAcylation: A sweet thorn in the spindle!Cell cycle (Georgetown, Tex.) · 2016
    Article
  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

5 authors at 1 institution in 1 country.

Ee Phie TanDepartment of Biochemistry and Molecular Biology.
Sarah CaroDepartment of Biochemistry and Molecular Biology.
Anish PotnisDepartment of Biochemistry and Molecular Biology.
Christopher LanzaDepartment of Biochemistry and Molecular Biology.
Chad SlawsonDepartment of Biochemistry and Molecular Biology; Department of KUMC Cancer Center; Institute for Reproductive Health and Regenerative Medicine, University of Kansas Medical Center, Kansas City, Kansas 64108. Electronic address: cslawson@kumc.edu.
University of Kansas Medical Center · US

Funding

NIGMS NIH HHS P20GM12345
6 · The paper itself

Abstract

Any defects in the correct formation of the mitotic spindle will lead to chromosomal segregation errors, mitotic arrest, or aneuploidy. We demonstrate that O-linked N-acetylglucosamine (O-GlcNAc), a post-translational modification of serine and threonine residues in nuclear and cytoplasmic proteins, regulates spindle function. In O-GlcNAc transferase or O-GlcNAcase gain of function cells, the mitotic spindle is incorrectly assembled. Chromosome condensation and centrosome assembly is impaired in these cells. The disruption in spindle architecture is due to a reduction in histone H3 phosphorylation by Aurora kinase B. However, gain of function cells treated with the O-GlcNAcase inhibitor Thiamet-G restored the assembly of the spindle and partially rescued histone phosphorylation. Together, these data suggest that the coordinated addition and removal of O-GlcNAc, termed O-GlcNAc cycling, regulates mitotic spindle organization and provides a potential new perspective on how O-GlcNAc regulates cellular events.

Indexed as

Acetylglucosaminebeta-N-AcetylhexosaminidasesChromosomes, HumanEnzyme InhibitorsGlucosyltransferasesHeLa CellsHistonesHumansPhosphorylationProtein Processing, Post-TranslationalPyransSpindle ApparatusThiazolesAcetylglucosaminebeta-N-AcetylhexosaminidasesEnzyme InhibitorsGlucosyltransferasesHistonesPyransthiamet GThiazolesCell CycleGlycosylationMitosisMitotic SpindlePhosphorylation

Identifiers

PMID23946484
PMCPMC3779708
OpenAlexW1999113688

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.