ArticleThe Journal of biological chemistry2015
O-fucose monosaccharide of Drosophila Notch has a temperature-sensitive function and cooperates with O-glucose glycan in Notch transport and Notch signaling activation.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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31 citing papers in PubMed, 48 citations in OpenAlex.
- Dynamic remodeling of membrane proteins for temperature adaptation in oysters.Zoological research · 2026Article
- Numb Suppresses Notch-Dependent Activation ofBiomolecules · 2024Article
- Fucose as a nutrient ligand for Dikarya and a building block of early diverging lineages.IMA fungus · 2023Article
- POFUT1 promotes gastric cancer progression through Notch/Wnt dual signaling pathways dependent on the parafibromin-NICD1-β-catenin complex.Journal of the Chinese Medical Association : JCMA · 2023Article
- Multifaceted regulation of Notch signaling by glycosylation.Glycobiology · 2021Review
- Other Types of Glycosylation.Advances in experimental medicine and biology · 2021Article
- Spatial regulation and generation of diversity in signaling pathways.Journal of biosciences · 2021Review
- RNAi-Mediated Silencing of Pgants Shows Core 1Frontiers in physiology · 2021Article
- Synthesis and biological roles of O-glycans in insects.Glycoconjugate journal · 2020Review
- Functional analysis of glycosylation using Drosophila melanogaster.Glycoconjugate journal · 2020Review
- Making sense out of missense mutations: Mechanistic dissection of Notch receptors through structure-function studies in Drosophila.Development, growth & differentiation · 2020Review
- Decoding the PTM-switchboard of Notch.Biochimica et biophysica acta. Molecular cell research · 2019Review
- Protein O-fucosylation: structure and function.Current opinion in structural biology · 2019Review
- Meeting Between Rumi and Shams in Notch Signaling; Implications for Pain Management: A Narrative Review.Anesthesiology and pain medicine · 2019Review
- Structures and functions of invertebrate glycosylation.Open biology · 2019Review
- Multiple roles for O-glycans in Notch signalling.FEBS letters · 2018Review
- Congenital diseases caused by defectiveNagoya journal of medical science · 2018Review
- Insight into Notch Signaling Steps That InvolveGenetics · 2018Article
- Tyrosine phosphorylation and proteolytic cleavage of Notch are required for non-canonical Notch/Abl signaling inDevelopment (Cambridge, England) · 2018Article
- Clinical significance and biological function of fucosyltransferase 2 in lung adenocarcinoma.Oncotarget · 2017Article
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Notch (N) is a transmembrane receptor that mediates the cell-cell interactions necessary for many cell fate decisions. N has many epidermal growth factor-like repeats that are O-fucosylated by the protein O-fucosyltransferase 1 (O-Fut1), and the O-fut1 gene is essential for N signaling. However, the role of the monosaccharide O-fucose on N is unclear, because O-Fut1 also appears to have O-fucosyltransferase activity-independent functions, including as an N-specific chaperon. Such an enzymatic activity-independent function could account for the essential role of O-fut1 in N signaling. To evaluate the role of the monosaccharide O-fucose modification in N signaling, here we generated a knock-in mutant of O-fut1 (O-fut1(R245A knock-in)), which expresses a mutant protein that lacks O-fucosyltransferase activity but maintains the N-specific chaperon activity. Using O-fut1(R245A knock-in) and other gene mutations that abolish the O-fucosylation of N, we found that the monosaccharide O-fucose modification of N has a temperature-sensitive function that is essential for N signaling. The O-fucose monosaccharide and O-glucose glycan modification, catalyzed by Rumi, function redundantly in the activation of N signaling. We also showed that the redundant function of these two modifications is responsible for the presence of N at the cell surface. Our findings elucidate how different forms of glycosylation on a protein can influence the protein's functions.
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