Evidence map›Paper›PMID 18840611›Full record

ArticleThe Journal of biological chemistry2008

O-linked beta-N-acetylglucosaminyltransferase substrate specificity is regulated by myosin phosphatase targeting and other interacting proteins.

Win D Cheung, Kaoru Sakabe, Michael P Housley, Wagner B Dias, 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 101 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed, 1 pooled it
5.0field-weighted citation impact, top 4% 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

101 citing papers in PubMed, 1 synthesis or guideline pooled it, 158 citations in OpenAlex.

  1. Pooled it
  2. International journal of molecular sciences · 2025
    Review
  3. Article
  4. Review
  5. The emerging role of CARM1 in cancer.Cellular oncology (Dordrecht, Netherlands) · 2024
    Review
  6. Review
  7. Review
  8. O-GlcNAcylation in ischemic diseases.Frontiers in pharmacology · 2024
    Review
  9. Review
  10. Review
  11. Article
  12. Protein arginine methylation in viral infection and antiviral immunity.International journal of biological sciences · 2023
    Review
  13. Review
  14. O-GlcNAcylation in Renal (Patho)Physiology.International journal of molecular sciences · 2022
    Review
  15. Review
  16. Advances in chemical probing of proteinChemical Society reviews · 2021
    Review
  17. Article
  18. Article
  19. Mammalian cell proliferation requires noncatalytic functions of O-GlcNAc transferase.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  20. The Journal of biological chemistry · 2020
    Article

41 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

5 authors at 2 institutions in 1 country.

Win D CheungDepartment of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205-2185, USA.
Kaoru Sakabe
Michael P Housley
Wagner B Dias
Gerald W Hart
Johns Hopkins University · USJohns Hopkins Medicine · 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
PROTEOGLYCANS AND GLYCOPROTEINS OF DEVELOPING THYMUSR01HD013563 · NICHD · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI HART, GERALD WARREN · 1985 to 1997
–
NCI NIH HHS R01 CA42486NICHD NIH HHS R01 HD13563
6 · The paper itself

Abstract

O-GlcNAc-transferase (OGT) substrate specificity is regulated by transiently interacting proteins. To further examine the regulation of OGT, we have identified 27 putative OGT-interacting proteins through a yeast two-hybrid screen. Two of these proteins, Trak1 (OIP106) and O-GlcNAcase, have been shown previously to interact with and regulate OGT. We demonstrate here that MYPT1 and CARM1 also interact with and target OGT. MYPT1 and CARM1 are substrates of OGT in vitro and in vivo. MYPT1 and CARM1 also function to alter OGT substrate specificity in vitro. Furthermore depletion of MYPT1 in Neuro-2a neuroblastoma cells alters GlcNAcylation of several proteins under basal conditions, suggesting that MYPT1 regulates OGT substrate specificity in vivo.

Indexed as

Gene Expression Regulation, EnzymologicAdaptor Proteins, Vesicular TransportAnimalsCarrier ProteinsCell Line, TumorHumansMiceModels, BiologicalMyosin-Light-Chain KinaseMyosin-Light-Chain PhosphataseN-AcetylglucosaminyltransferasesProtein BindingProtein Structure, TertiaryRNA Polymerase IISubstrate SpecificityTwo-Hybrid System TechniquesAdaptor Proteins, Vesicular TransportCarrier ProteinsMyosin-Light-Chain KinaseMyosin-Light-Chain PhosphataseN-AcetylglucosaminyltransferasesPpp1r12a protein, mouseRNA Polymerase IITrak1 protein, mouse

Identifiers

PMID18840611
PMCPMC2590692
OpenAlexW2113379985

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.