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Article

Chaperone activity of protein O-fucosyltransferase 1 promotes notch receptor folding.

Science (New York, N.Y.) - 11 Mar 2005

Okajima Tetsuya, Xu Aiguo, Lei Liang, Irvine Kenneth D

Abstract excerpt

Notch proteins are receptors for a conserved signaling pathway that affects numerous cell fate decisions. We found that in Drosophila, Protein O-fucosyltransferase 1 (OFUT1), an enzyme that glycosylates epidermal growth factor-like domains of Notch, also has a distinct Notch chaperone activity. OFUT1 is an endoplasmic reticulum protein, and its localization was essential for function in vivo. OFUT1 could bind to...

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Identifiers

PMID: 15692013
DOI: 10.1126/science.1108995

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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Chaperone activity of protein O-fucosyltransferase 1 promotes notch receptor folding.PMID 15692013Read ↗

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The balance between GMD and OFUT1 regulates Notch signaling pathway activity by modulating Notch stability.Semantic proximity Read ↗

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Contribution of extracellular O-GlcNAc to the stability of folded epidermal growth factor-like domains and Notch1 trafficking.Semantic proximity Read ↗

Ero1L, a thiol oxidase, is required for Notch signaling through cysteine bridge formation of the Lin12-Notch repeats in Drosophila melanogaster.Semantic proximity Read ↗

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