Evidence map›Paper›PMID 19506079›Full record

ArticleThe Journal of biological chemistry2009

Regulation of calcium/calmodulin-dependent kinase IV by O-GlcNAc modification.

Wagner B Dias, Win D Cheung, Zihao Wang, Gerald W Hart

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.

0numbers the graph read from it
0cells of the map it votes in
91citing papers in PubMed
3.1field-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

91 citing papers in PubMed, 150 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Review
  7. International journal of molecular sciences · 2025
    Review
  8. Article
  9. Review
  10. Review
  11. The O-GlcNAc dichotomy: when does adaptation become pathological?Clinical science (London, England : 1979) · 2023
    Review
  12. Article
  13. Article
  14. The role of O-GlcNAcylation in development.Development (Cambridge, England) · 2023
    Article
  15. Frontiers in endocrinology · 2023
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

31 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

4 authors at 2 institutions in 1 country.

Wagner B DiasDepartment of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
Win D Cheung
Zihao Wang
Gerald W Hart
Johns Hopkins Medicine · USJohns Hopkins University · US

Funding

ROLE OF CELL-SURFACE SIALYLATION IN TUMOR METASTASISR01CA042486 · NCI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI HART, GERALD WARREN · 1986 to 2013
$4.9M
Cytosolic O-Glycosylation and Insulin SignalingR01DK061671 · NIDDK · JOHNS HOPKINS UNIVERSITY · PI HART, GERALD WARREN · 2002 to 2014
$4.0M
NHLBI PROTEOMICS INITIATIVE-N01HV28180-268028180-268028180N01HV028180 · HV · JOHNS HOPKINS UNIVERSITY · PI VAN EYK, JENNIFER E · 2002 to 2006
–
NCI NIH HHS CA42486NCI NIH HHS R01 CA042486NHLBI NIH HHS N01 HV028180NHLBI NIH HHS N01-HV-28180NIDDK NIH HHS DK61671NIDDK NIH HHS R01 DK061671
6 · The paper itself

Abstract

Similar to phosphorylation, GlcNAcylation (the addition of O-GlcNAc to Ser(Thr) residues on polypeptides) is an abundant, dynamic, and inducible post-translational modification. GlcNAcylated proteins are crucial in regulating virtually all cellular processes, including signaling, cell cycle, and transcription. Here we show that calcium/calmodulin-dependent kinase IV (CaMKIV) is highly GlcNAcylated in vivo. In addition, we show that upon activation of HEK293 cells, hemagglutinin-tagged CaMKIV GlcNAcylation rapidly decreases, in a manner directly opposing its phosphorylation at Thr-200. Correspondingly, there is an increase in CaMKIV interaction with O-GlcNAcase during CaMKIV activation. Furthermore, we identify at least five sites of GlcNAcylation on CaMKIV. Using site-directed mutagenesis, we determine that the GlcNAcylation sites located in the active site of CaMKIV can modulate its phosphorylation at Thr-200 and its activity toward cAMP-response element-binding transcription factor. Our results strongly indicate that the O-GlcNAc modification participates in the regulation of CaMKIV activation and function, possibly coordinating nutritional signals with the immune and nervous systems. This is the first example of an O-GlcNAc/phosphate cycle involving O-GlcNAc transferase/kinase cross-talk.

Indexed as

Gene Expression Regulation, EnzymologicAcetylglucosamineAnimalsCalcium-Calmodulin-Dependent Protein KinasesCalcium-Calmodulin-Dependent Protein Kinase Type 4Cell LineCerebellumHumansModels, BiologicalMutagenesis, Site-DirectedPhosphorylationProtein Structure, TertiaryRatsThreonineAcetylglucosamineCalcium-Calmodulin-Dependent Protein KinasesCalcium-Calmodulin-Dependent Protein Kinase Type 4CAMK4 protein, humanCamk4 protein, ratThreonine

Identifiers

PMID19506079
PMCPMC2755857
OpenAlexW2004914600

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.