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O-Linked-N-acetylglucosamine on extracellular protein domains mediates epithelial cell–matrix interactions

Author

Listed:
  • Yuta Sakaidani

    (Nagoya University Graduate School of Medicine
    Nagoya University Graduate School of Bioagricultural Sciences)

  • Tomoko Nomura

    (Nagoya University Graduate School of Medicine)

  • Aiko Matsuura

    (Nagoya University Graduate School of Bioagricultural Sciences)

  • Makiko Ito

    (Nagoya University Graduate School of Bioagricultural Sciences)

  • Emiko Suzuki

    (Structural Biology Center, National Institute of Genetics, The Graduate University for Advanced Studies)

  • Kosuke Murakami

    (Nagoya University Graduate School of Bioagricultural Sciences)

  • Daita Nadano

    (Nagoya University Graduate School of Bioagricultural Sciences)

  • Tsukasa Matsuda

    (Nagoya University Graduate School of Bioagricultural Sciences)

  • Koichi Furukawa

    (Nagoya University Graduate School of Medicine)

  • Tetsuya Okajima

    (Nagoya University Graduate School of Medicine
    Nagoya University Graduate School of Bioagricultural Sciences)

Abstract

The O-linked-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins regulates basic cellular functions and is involved in the aetiology of diabetes and neurodegeneration. This intracellular O-GlcNAcylation is catalyzed by a single O-GlcNAc transferase, OGT. Here we report a novel OGT, EOGT, responsible for extracellular O-GlcNAcylation. Although both OGT and EOGT are regulated by hexosamine flux, EOGT localizes to the lumen of the endoplasmic reticulum and transfers GlcNAc to epidermal growth factor-like domains in an OGT-independent manner. Loss of Eogt gives phenotypes similar to those caused by defects in the apical extracellular matrix. Dumpy (Dp), a membrane-anchored extracellular protein, is O-GlcNAcylated, and EOGT is required for Dp-dependent epithelial cell–matrix interactions. Thus, O-GlcNAcylation of secreted and membrane glycoproteins is a novel mediator of cell–cell or cell–matrix interactions at the cell surface.

Suggested Citation

  • Yuta Sakaidani & Tomoko Nomura & Aiko Matsuura & Makiko Ito & Emiko Suzuki & Kosuke Murakami & Daita Nadano & Tsukasa Matsuda & Koichi Furukawa & Tetsuya Okajima, 2011. "O-Linked-N-acetylglucosamine on extracellular protein domains mediates epithelial cell–matrix interactions," Nature Communications, Nature, vol. 2(1), pages 1-9, September.
    • Handle: RePEc:nat:natcom:v:2:y:2011:i:1:d:10.1038_ncomms1591
    DOI: 10.1038/ncomms1591
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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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