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

Yuta Sakaidani, Tomoko Nomura, Aiko Matsuura, Makiko Ito, Emiko Suzuki, Kosuke Murakami, Daita Nadano, Tsukasa Matsuda, Koichi Furukawa and Tetsuya Okajima ()
Additional contact information
Yuta Sakaidani: Nagoya University Graduate School of Medicine
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

Nature Communications, 2011, vol. 2, issue 1, 1-9

Abstract: 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.

Date: 2011
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/ncomms1591 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:2:y:2011:i:1:d:10.1038_ncomms1591

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms1591

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().