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Glycosyltransferase activity of Fringe modulates Notch–Delta interactions

Author

Listed:
  • Katja Brückner

    (European Molecular Biology Laboratory
    Howard Hughes Medical Institute)

  • Lidia Perez

    (European Molecular Biology Laboratory)

  • Henrik Clausen

    (School of Dentistry, University of Copenhagen)

  • Stephen Cohen

    (European Molecular Biology Laboratory)

Abstract

Ligands that are capable of activating Notch family receptors are broadly expressed in animal development, but their activity is tightly regulated to allow formation of tissue boundaries1. Members of the fringe gene family have been implicated in limiting Notch activation during boundary formation2,3,4,5,6,7,8, but the mechanism of Fringe function has not been determined. Here we present evidence that Fringe acts in the Golgi as a glycosyltransferase enzyme that modifies the epidermal growth factor (EGF) modules of Notch and alters the ability of Notch to bind its ligand Delta. Fringe catalyses the addition of N-acetylglucosamine to fucose, which is consistent with a role in the elongation of O-linked fucose O-glycosylation that is associated with EGF repeats. We suggest that cell-type-specific modification of glycosylation may provide a general mechanism to regulate ligand–receptor interactions in vivo.

Suggested Citation

  • Katja Brückner & Lidia Perez & Henrik Clausen & Stephen Cohen, 2000. "Glycosyltransferase activity of Fringe modulates Notch–Delta interactions," Nature, Nature, vol. 406(6794), pages 411-415, July.
    • Handle: RePEc:nat:nature:v:406:y:2000:i:6794:d:10.1038_35019075
    DOI: 10.1038/35019075
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    Cited by:

    1. Yue Li & Tianfeng Lu & Pengzhen Dong & Jian Chen & Qiang Zhao & Yuying Wang & Tianheng Xiao & Honggang Wu & Quanyi Zhao & Hai Huang, 2024. "A single-cell atlas of Drosophila trachea reveals glycosylation-mediated Notch signaling in cell fate specification," Nature Communications, Nature, vol. 15(1), pages 1-18, December.

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