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

Structural analysis of Notch-regulating Rumi reveals basis for pathogenic mutations.

Nature chemical biology - 1 Sept 2016

Yu Hongjun, Takeuchi Hideyuki, Takeuchi Megumi, Liu Qun, Kantharia Joshua, Haltiwanger Robert S, Li Huilin

Abstract excerpt

Rumi O-glucosylates the EGF repeats of a growing list of proteins essential in metazoan development, including Notch. Rumi is essential for Notch signaling, and Rumi dysregulation is linked to several human diseases. Despite Rumi's critical roles, it is unknown how Rumi glucosylates a serine of many but not all EGF repeats. Here we report crystal structures of Drosophila Rumi as binary and ternary complexes with...

Read the complete abstract on PubMed

Topics

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

Share to Biocatalysis
Share to Drosophila melanogaster

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Drosophila Proteins

Share to EGF gene

Share to Glucosyltransferases

Share to Mutation

Share to Protein Conformation

Source

Open in PubMed Open full text

Identifiers

PMID: 27428513
DOI: 10.1038/nchembio.2135
PMCID: PMC4990500

Genes

EGF

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural analysis of Notch-regulating Rumi reveals basis for pathogenic mutations.PMID 27428513Read ↗

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

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

Rumi is a CAP10 domain glycosyltransferase that modifies Notch and is required for Notch signaling.Semantic proximity Read ↗

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

A notch sweeter.Semantic proximity Read ↗

Structure-function analysis of Drosophila Notch using genomic rescue transgenes.Semantic proximity Read ↗

Molecular genetic analysis of the glycosyltransferase Fringe in Drosophila.Semantic proximity Read ↗

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

NGLY1: A fascinating, multifunctional molecule.Semantic proximity Read ↗

Structural and mechanistic insights into lunatic fringe from a kinetic analysis of enzyme mutants.Semantic proximity Read ↗

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

Mutations in four glycosyl hydrolases reveal a highly coordinated pathway for rhodopsin biosynthesis and N-glycan trimming in Drosophila melanogaster.Semantic proximity Read ↗

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