Evidence map›Paper›PMID 18420577›Full record

ArticleThe Journal of biological chemistry2008

O-GlcNAc regulates FoxO activation in response to glucose.

Michael P Housley, Joseph T Rodgers, Namrata D Udeshi, Timothy J Kelly, Jeffrey Shabanowitz, Donald F Hunt, Pere Puigserver, Gerald W Hart

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 197 papers.

0numbers the graph read from it
0cells of the map it votes in
197citing papers in PubMed
9.5field-weighted citation impact, top 1% 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

197 citing papers in PubMed, 325 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. PKCβ II antagonizes O-GlcNAcylated FOXO4 and inhibits lipid synthesis.Apoptosis : an international journal on programmed cell death · 2026
    Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Structural glycobiology - from enzymes to organelles.Biochemical Society transactions · 2025
    Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. Review
  19. Review
  20. Review

137 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

8 authors at 5 institutions in 1 country.

Michael P HousleyDepartment of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
Joseph T Rodgers
Namrata D Udeshi
Timothy J Kelly
Jeffrey Shabanowitz
Donald F Hunt
Pere Puigserver
Gerald W Hart
Harvard University · USDana-Farber Cancer Institute · USJohns Hopkins Medicine · USJohns Hopkins University · USUniversity of Virginia · US

Funding

PROTEIN SEQUENCING BY TANDEM MASS SPECTROMETRYR01GM037537 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI HUNT, DONALD F · 1987 to 2023
$17.8M
Cytosolic O-Glycosylation and Insulin SignalingR01DK061671 · NIDDK · JOHNS HOPKINS UNIVERSITY · PI HART, GERALD WARREN · 2002 to 2014
$4.0M
GLYCOCONJUGATES IN DEVELOPMENT AND IMMUNITYR37HD013563 · NICHD · JOHNS HOPKINS UNIVERSITY · PI HART, GERALD WARREN · 1998 to 2007
$3.4M
PROTEOGLYCANS AND GLYCOPROTEINS OF DEVELOPING THYMUSR01HD013563 · NICHD · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI HART, GERALD WARREN · 1985 to 1997
–
NICHD NIH HHS HD13563NICHD NIH HHS R37 HD013563NIDDK NIH HHS DK61671NIDDK NIH HHS R01 DK061671NIGMS NIH HHS GM37537NIGMS NIH HHS R01 GM037537
6 · The paper itself

Abstract

FoxO proteins are key transcriptional regulators of nutrient homeostasis and stress response. The transcription factor FoxO1 activates expression of gluconeogenic, including phosphoenolpyruvate carboxykinase and glucose-6-phosphatase, and also activates the expression of the oxidative stress response enzymes catalase and manganese superoxide dismutase. Hormonal and stress-dependent regulation of FoxO1 via acetylation, ubiquitination, and phosphorylation, are well established, but FoxOs have not been studied in the context of the glucose-derived O-linked beta-N-acetylglucosamine (O-GlcNAc) modification. Here we show that O-GlcNAc on hepatic FoxO1 is increased in diabetes. Furthermore, O-GlcNAc regulates FoxO1 activation in response to glucose, resulting in the paradoxically increased expression of gluconeogenic genes while concomitantly inducing expression of genes encoding enzymes that detoxify reactive oxygen species. GlcNAcylation of FoxO provides a new mechanism for direct nutrient control of transcription to regulate metabolism and stress response through control of FoxO1 activity.

Indexed as

Gene Expression RegulationAcetylglucosamineAnimalsCatalaseDiabetes Mellitus, ExperimentalForkhead Box Protein O1Forkhead Transcription FactorsGlucoseGlucose-6-PhosphataseHumansModels, BiologicalNerve Tissue ProteinsPhosphoenolpyruvate Carboxykinase (ATP)RatsReactive Oxygen SpeciesSuperoxide DismutaseAcetylglucosamineCatalaseForkhead Box Protein O1Forkhead Transcription FactorsFOXO1 protein, humanFoxo1 protein, ratGlucoseGlucose-6-PhosphataseNerve Tissue ProteinsPhosphoenolpyruvate Carboxykinase (ATP)Reactive Oxygen SpeciesSuperoxide Dismutase

Identifiers

PMID18420577
PMCPMC2423255
OpenAlexW2062236151

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.