Evidence map›Paper›PMID 20805223›Full record

ArticleThe Journal of biological chemistry2010

O-GlcNAc transferase regulates mitotic chromatin dynamics.

Kaoru Sakabe, Gerald W Hart

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed, 1 pooled it
3.9field-weighted citation impact, top 6% 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

88 citing papers in PubMed, 1 synthesis or guideline pooled it, 131 citations in OpenAlex.

  1. Interplay Between Glucose Metabolism and Chromatin Modifications in Cancer.Frontiers in cell and developmental biology · 2021
    Pooled it
  2. Review
  3. Review
  4. Article
  5. The emerging role of CARM1 in cancer.Cellular oncology (Dordrecht, Netherlands) · 2024
    Review
  6. Review
  7. Review
  8. The O-GlcNAc dichotomy: when does adaptation become pathological?Clinical science (London, England : 1979) · 2023
    Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Review
  18. Structure, Activity, and Function of PRMT1.Life (Basel, Switzerland) · 2021
    Review
  19. Review
  20. Review

28 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Kaoru SakabeDepartment of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
Gerald W Hart
Johns Hopkins Medicine · US

Funding

JHU-UMD Diabetes Research CenterP30DK079637 · NIDDK · JOHNS HOPKINS UNIVERSITY · PI AHIMA, REXFORD S. · 2013 to 2017
$9.7M
Cytosolic O-Glycosylation and Insulin SignalingR01DK061671 · NIDDK · JOHNS HOPKINS UNIVERSITY · PI HART, GERALD WARREN · 2002 to 2014
$4.0M
NCI NIH HHS R01 CA2486NIDDK NIH HHS P30 DK079637NIDDK NIH HHS R01 DK061671NIDDK NIH HHS R01 DK61671
6 · The paper itself

Abstract

Mitosis must faithfully divide the genome such that each progeny inherits the same genetic material. DNA condensation is crucial in ensuring that chromosomes are correctly attached to the mitotic spindle for segregation, preventing DNA breaks or constrictions from the contractile ring. Histones form an octameric complex of basic proteins important in regulating DNA organization and accessibility. Histone post-translational modifications are altered during mitosis, although the roles of these post-translational modifications remain poorly characterized. Here, we report that N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme catalyzing the addition of O-GlcNAc moieties to nuclear and cytoplasmic proteins at serine and threonine residues, regulates some aspects of mitotic chromatin dynamics. OGT protein amounts decrease during M phase. Modest overexpression of OGT alters mitotic histone post-translational modifications at Lys-9, Ser-10, Arg-17, and Lys-27 of histone H3. Overexpression of OGT also prevents mitotic phosphorylation of coactivator-associated arginine methyltransferase 1 (CARM1) and prevents its correct cellular localization during mitosis. Moreover, OGT overexpression results in an increase in abnormal chromosomal bridge formation. Together, these results show that regulating the amount of OGT during mitosis is important in ensuring correct chromosomal segregation during mitosis.

Indexed as

ChromatinChromatin Assembly and DisassemblyChromosome SegregationChromosomes, HumanDNA BreaksGene Expression Regulation, EnzymologicGenome, HumanHeLa CellsHistonesHumansMitosisN-AcetylglucosaminyltransferasesProtein-Arginine N-MethyltransferasesProtein Processing, Post-TranslationalProtein TransportSpindle ApparatusChromatincoactivator-associated arginine methyltransferase 1HistonesN-AcetylglucosaminyltransferasesProtein-Arginine N-Methyltransferases

Identifiers

PMID20805223
PMCPMC2966060
OpenAlexW2093664191

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.