Evidence map›Paper›PMID 26674417›Full record

ArticleOpen biology2015

Dual functionality of O-GlcNAc transferase is required for Drosophila development.

Daniel Mariappa, Xiaowei Zheng, Marianne Schimpl, Olawale Raimi, Andrew T Ferenbach, H-Arno J Müller, Daan M F van Aalten

Open access · goldAbstract read
In one paragraph

Article in Open biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

19 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Article
  3. Phage display uncovers a sequence motif that drives polypeptide binding to a conserved regulatory exosite of O-GlcNAc transferase.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. The role of O-GlcNAcylation in development.Development (Cambridge, England) · 2023
    Article
  5. Review
  6. Article
  7. Cells · 2022
    Review
  8. Article
  9. Review
  10. 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
  11. Article
  12. Catalytic deficiency of O-GlcNAc transferase leads to X-linked intellectual disability.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  13. A complex containing theThe Journal of biological chemistry · 2019
    Article
  14. Regulation of Polycomb Repression byFrontiers in endocrinology · 2019
    Review
  15. The Journal of biological chemistry · 2018
    Article
  16. Effects of hypo-The Journal of biological chemistry · 2018
    Article
  17. Mutations inThe Journal of biological chemistry · 2017
    Article
  18. Article
  19. Review
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

7 authors at 2 institutions in 1 country.

Daniel MariappaMRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.
Xiaowei ZhengMRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.
Marianne SchimplMRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.
Olawale RaimiDivision of Molecular Microbiology, University of Dundee, Dundee, UK.
Andrew T FerenbachMRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.
H-Arno J MüllerDivision of Cell and Developmental Biology, College of Life Sciences, University of Dundee, Dundee, UK.
Daan M F van AaltenMRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK Division of Molecular Microbiology, University of Dundee, Dundee, UK dmfvanaalten@dundee.ac.uk.
University of Dundee · GBMRC Protein Phosphorylation and Ubiquitylation Unit · GB

Funding

Medical Research Council G0501679Medical Research Council MR/K015869/1Medical Research Council MR/K018531/1Wellcome Trust 087590Wellcome Trust 097945Wellcome Trust 097945/B/11/ZWellcome Trust WT087590MA
6 · The paper itself

Abstract

Post-translational modification of intracellular proteins with O-linked N-acetylglucosamine (O-GlcNAc) catalysed by O-GlcNAc transferase (OGT) has been linked to regulation of diverse cellular functions. OGT possesses a C-terminal glycosyltransferase catalytic domain and N-terminal tetratricopeptide repeats that are implicated in protein-protein interactions. Drosophila OGT (DmOGT) is encoded by super sex combs (sxc), mutants of which are pupal lethal. However, it is not clear if this phenotype is caused by reduction of O-GlcNAcylation. Here we use a genetic approach to demonstrate that post-pupal Drosophila development can proceed with negligible OGT catalysis, while early embryonic development is OGT activity-dependent. Structural and enzymatic comparison between human OGT (hOGT) and DmOGT informed the rational design of DmOGT point mutants with a range of reduced catalytic activities. Strikingly, a severely hypomorphic OGT mutant complements sxc pupal lethality. However, the hypomorphic OGT mutant-rescued progeny do not produce F2 adults, because a set of Hox genes is de-repressed in F2 embryos, resulting in homeotic phenotypes. Thus, OGT catalytic activity is required up to late pupal stages, while further development proceeds with severely reduced OGT activity.

Indexed as

AnimalsDrosophilaDrosophila ProteinsHumansN-AcetylglucosaminyltransferasesProtein ConformationSubstrate SpecificityDrosophila ProteinsN-AcetylglucosaminyltransferasesO-GlcNAc transferaseDrosophila developmentHoxO-GlcNAcO-GlcNAc transferase

Identifiers

PMID26674417
PMCPMC4703063
OpenAlexW2207926632

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.