Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The EGF repeat-specific O-GlcNAc-transferase Eogt interacts with notch signaling and pyrimidine metabolism pathways in Drosophila.

PloS one - 1 Jan 2013

Müller Reto, Jenny Andreas, Stanley Pamela

Abstract excerpt

The O-GlcNAc transferase Eogt modifies EGF repeats in proteins that transit the secretory pathway, including Dumpy and Notch. In this paper, we show that the Notch ligands Delta and Serrate are also substrates of Eogt, that mutation of a putative UDP-GlcNAc binding DXD motif greatly reduces enzyme activity, and that Eogt and the cytoplasmic O-GlcNAc transferase Ogt have distinct substrates in Drosophila larvae....

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Motifs
Share to Gene Knockdown Techniques
Share to Larva

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to N-Acetylglucosaminyltransferases

Share to Pyrimidines

Share to Receptors, Notch

Share to Uracil

Share to Wings, Animal

Source

Open in PubMed Open full text

Identifiers

PMID: 23671640
DOI: 10.1371/journal.pone.0062835
PMCID: PMC3650022

Genes

EGF

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The EGF repeat-specific O-GlcNAc-transferase Eogt interacts with notch signaling and pyrimidine metabolism pathways in Drosophila.PMID 23671640Read ↗

EOGT and O-GlcNAc on secreted and membrane proteins.Semantic proximity Read ↗

N-acetylglucosamine modification in the lumen of the endoplasmic reticulum.Semantic proximity Read ↗

Regulation of mammalian Notch signaling and embryonic development by the protein O-glucosyltransferase Rumi.Semantic proximity Read ↗

Impaired O-linked N-acetylglucosaminylation in the endoplasmic reticulum by mutated epidermal growth factor (EGF) domain-specific O-linked N-acetylglucosamine transferase found in Adams-Oliver syndrome.Semantic proximity Read ↗

Structural analysis of Notch-regulating Rumi reveals basis for pathogenic mutations.Semantic proximity Read ↗

Negative regulation of notch signaling by xylose.Semantic proximity Read ↗

Rumi functions as both a protein O-glucosyltransferase and a protein O-xylosyltransferase.Semantic proximity Read ↗

Two pathways for importing GDP-fucose into the endoplasmic reticulum lumen function redundantly in the O-fucosylation of Notch in Drosophila.Semantic proximity Read ↗

Rescue of Notch signaling in cells incapable of GDP-L-fucose synthesis by gap junction transfer of GDP-L-fucose in Drosophila.Semantic proximity Read ↗

The gene Serrate encodes a putative EGF-like transmembrane protein essential for proper ectodermal development in Drosophila melanogaster.Semantic proximity Read ↗

Multiple O-glucosylation sites on Notch function as a buffer against temperature-dependent loss of signaling.Semantic proximity Read ↗

Phenotype-based clustering of glycosylation-related genes by RNAi-mediated gene silencing.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.