ArticlePLoS genetics2015
Protein O-Glucosyltransferase 1 (POGLUT1) Promotes Mouse Gastrulation through Modification of the Apical Polarity Protein CRUMBS2.
Article in PLoS genetics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 39 citations in OpenAlex.
- ER quality control of Crumbs2 and Notch proteins by GXYLT1-dependent xylosyl elongation of O-glucose glycans.The Journal of biological chemistry · 2026Article
- The glycosyltransferase POGLUT1 regulates muscle stem cell development and maintenance in mice.PLoS genetics · 2025Article
- The Lego hypothesis of tissue morphogenesis: stereotypic organization of parallel orientational cell adhesions for epithelial self-assembly.Biological reviews of the Cambridge Philosophical Society · 2025Review
- The glycosyltransferase POGLUT1 regulates muscle stem cell development and maintenance in mice.bioRxiv : the preprint server for biology · 2024Article
- Disease modeling and gene correction of LGMDR21 iPSCs elucidates the role of POGLUT1 in skeletal muscle maintenance, regeneration, and the satellite cell niche.Molecular therapy. Nucleic acids · 2023Article
- Structure, function, and pathology of protein O-glucosyltransferases.Cell death & disease · 2021Review
- Multifaceted regulation of Notch signaling by glycosylation.Glycobiology · 2021Review
- Other Types of Glycosylation.Advances in experimental medicine and biology · 2021Article
- Asymmetry in the frequency and position of mitosis in the mouse embryo epiblast at gastrulation.EMBO reports · 2020Article
- The Epithelial-to-Mesenchymal Transition (EMT) in Development and Cancer.Annual review of cancer biology · 2020Article
- Crumbs2 mediates ventricular layer remodelling to form the spinal cord central canal.PLoS biology · 2020Article
- Decoding the PTM-switchboard of Notch.Biochimica et biophysica acta. Molecular cell research · 2019Review
- Multiple roles for O-glycans in Notch signalling.FEBS letters · 2018Review
- Sensitized genetic backgrounds reveal differential roles for EGF repeat xylosyltransferases in Drosophila Notch signaling.Glycobiology · 2018Article
- Expression and localization of the polarity protein CRB2 in adult mouse brain: a comparison with the CRB1Scientific reports · 2018Article
- A dual role of the extracellular domain ofBiology open · 2018Article
- Article
- STRIP1, a core component of STRIPAK complexes, is essential for normal mesoderm migration in the mouse embryo.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Structural basis of Notch O-glucosylation and O-xylosylation by mammalian protein-O-glucosyltransferase 1 (POGLUT1).Nature communications · 2017Article
- The Crumbs_C isoform ofBiology open · 2017Article
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Authors and funding
10 authors at 7 institutions in 3 countries.
Funding
Abstract
Crumbs family proteins are apical transmembrane proteins with ancient roles in cell polarity. Mouse Crumbs2 mutants arrest at midgestation with abnormal neural plate morphology and a deficit of mesoderm caused by defects in gastrulation. We identified an ENU-induced mutation, wsnp, that phenocopies the Crumbs2 null phenotype. We show that wsnp is a null allele of Protein O-glucosyltransferase 1 (Poglut1), which encodes an enzyme previously shown to add O-glucose to EGF repeats in the extracellular domain of Drosophila and mammalian Notch, but the role of POGLUT1 in mammalian gastrulation has not been investigated. As predicted, we find that POGLUT1 is essential for Notch signaling in the early mouse embryo. However, the loss of mouse POGLUT1 causes an earlier and more dramatic phenotype than does the loss of activity of the Notch pathway, indicating that POGLUT1 has additional biologically relevant substrates. Using mass spectrometry, we show that POGLUT1 modifies EGF repeats in the extracellular domain of full-length mouse CRUMBS2. CRUMBS2 that lacks the O-glucose modification fails to be enriched on the apical plasma membrane and instead accumulates in the endoplasmic reticulum. The data demonstrate that CRUMBS2 is the target of POGLUT1 for the gastrulation epithelial-to-mesenchymal transitions (EMT) and that all activity of CRUMBS2 depends on modification by POGLUT1. Mutations in human POGLUT1 cause Dowling-Degos Disease, POGLUT1 is overexpressed in a variety of tumor cells, and mutations in the EGF repeats of human CRUMBS proteins are associated with human congenital nephrosis, retinitis pigmentosa and retinal degeneration, suggesting that O-glucosylation of CRUMBS proteins has broad roles in human health.
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