Evidence map›Paper›PMID 27268051›Full record

ArticleThe Journal of biological chemistry2016

Mapping Sites of O-Glycosylation and Fringe Elongation on Drosophila Notch.

Beth M Harvey, Nadia A Rana, Hillary Moss, Jessica Leonardi, Hamed Jafar-Nejad, Robert S Haltiwanger

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

39 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
  2. Review
  3. Nagoya journal of medical science · 2025
    Article
  4. Article
  5. ProteinMolecules (Basel, Switzerland) · 2025
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Glycans that regulate Notch signaling in the intestine.Biochemical Society transactions · 2022
    Review
  12. Significant Roles of NotchMolecules (Basel, Switzerland) · 2022
    Review
  13. Signalling dynamics in embryonic development.The Biochemical journal · 2021
    Review
  14. Article
  15. Current Views on the Roles ofBiomolecules · 2021
    Review
  16. Review
  17. Article
  18. Article
  19. Review
  20. 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

6 authors at 2 institutions in 1 country.

Beth M HarveyFrom the Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, New York 11794-5215.
Nadia A RanaFrom the Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, New York 11794-5215.
Hillary MossFrom the Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, New York 11794-5215.
Jessica Leonardithe Program in Developmental Biology, Baylor College of Medicine, Houston, Texas 77030, and.
Hamed Jafar-Nejadthe Program in Developmental Biology, Baylor College of Medicine, Houston, Texas 77030, and the Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, Texas 77030.
Robert S HaltiwangerFrom the Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, New York 11794-5215, rhalti@uga.edu.
Stony Brook University · USBaylor College of Medicine · US

Funding

Resource Component: Acquisition, maintenance and distribution of Drosophila stocksP40OD018537 · OD · TRUSTEES OF INDIANA UNIVERSITY · PI Annette L. Parks · 2014 to 2026
$13.5M
O-Glycosylation of Epidermal Growth Factor-like MotifsR01GM061126 · NIGMS · UNIVERSITY OF GEORGIA · PI HALTIWANGER, ROBERT S. · 2001 to 2021
$9.1M
Fine-Tuning the Notch Signaling Pathway via O-GlucosylationR01GM084135 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI JAFAR-NEJAD, HAMED · 2008 to 2017
$2.6M
MOLECULAR AND CELLULAR BIOLOGY TRAINING PROGRAMT32GM008468 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI NEIMAN, AARON M · 1997 to 2016
$1.9M
NIGMS NIH HHS R01 GM061126NIGMS NIH HHS R01 GM084135NIGMS NIH HHS T32 GM008468NIH HHS P40 OD018537
6 · The paper itself

Abstract

Glycosylation of the Notch receptor is essential for its activity and serves as an important modulator of signaling. Three major forms of O-glycosylation are predicted to occur at consensus sites within the epidermal growth factor-like repeats in the extracellular domain of the receptor: O-fucosylation, O-glucosylation, and O-GlcNAcylation. We have performed comprehensive mass spectral analyses of these three types of O-glycosylation on Drosophila Notch produced in S2 cells and identified peptides containing all 22 predicted O-fucose sites, all 18 predicted O-glucose sites, and all 18 putative O-GlcNAc sites. Using semiquantitative mass spectral methods, we have evaluated the occupancy and relative amounts of glycans at each site. The majority of the O-fucose sites were modified to high stoichiometries. Upon expression of the β3-N-acetylglucosaminyltransferase Fringe with Notch, we observed varying degrees of elongation beyond O-fucose monosaccharide, indicating that Fringe preferentially modifies certain sites more than others. Rumi modified O-glucose sites to high stoichiometries, although elongation of the O-glucose was site-specific. Although the current putative consensus sequence for O-GlcNAcylation predicts 18 O-GlcNAc sites on Notch, we only observed apparent O-GlcNAc modification at five sites. In addition, we performed mass spectral analysis on endogenous Notch purified from Drosophila embryos and found that the glycosylation states were similar to those found on Notch from S2 cells. These data provide foundational information for future studies investigating the mechanisms of how O-glycosylation regulates Notch activity.

Indexed as

Drosophila ProteinsN-AcetylglucosaminyltransferasesPeptide MappingPeptidesReceptors, NotchAnimalsCell LineDrosophila melanogasterFucoseGlycosylationDrosophila Proteinsfng protein, DrosophilaFucoseN-AcetylglucosaminyltransferasesN protein, DrosophilaPeptidesReceptors, NotchEGF repeatFringeglycosylationglycosyltransferasemass spectrometry (MS)Notch receptorO-linked fucoseO-linked glucoseO-linked N-acetylglucosamine (O-GlcNAc)

Identifiers

PMID27268051
PMCPMC4965582
OpenAlexW2411239746

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.