Structure and function of extracellular O-GlcNAc

Mitsutaka Ogawa; Tetsuya Okajima

doi:10.1016/j.sbi.2018.12.002

Structure and function of extracellular O-GlcNAc

Curr Opin Struct Biol. 2019 Jun:56:72-77. doi: 10.1016/j.sbi.2018.12.002. Epub 2019 Jan 19.

Authors

Mitsutaka Ogawa¹, Tetsuya Okajima²

Affiliations

¹ Department of Molecular Biochemistry, Nagoya University Graduate School of Medicine, 65 Tsurumai, Showa-ku, Nagoya 466-8550, Japan.
² Department of Molecular Biochemistry, Nagoya University Graduate School of Medicine, 65 Tsurumai, Showa-ku, Nagoya 466-8550, Japan. Electronic address: tokajima@med.nagoya-u.ac.jp.

PMID: 30669087
DOI: 10.1016/j.sbi.2018.12.002

Abstract

Extracellular O-GlcNAc is a unique modification restricted to the epidermal growth factor (EGF) domain-containing glycoproteins. This O-GlcNAcylation is catalyzed by the EGF-domain specific O-GlcNAc transferase (EOGT), which is localized in the lumen of endoplasmic reticulum. In humans, EOGT is one of the causative genes of a congenital disease, Adams-Oliver syndrome. EOGT is highly expressed in endothelial cells and regulates vascular development and integrity by potentiating Delta-like ligand-mediated Notch signaling. In Drosophila, Eogt modifies Dumpy, an apical extracellular matrix glycoprotein, and affects Dumpy-dependent cell-matrix interaction. In this review, we summarize the current findings of the structure and functions of extracellular O-GlcNAc in animals.

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

Acetylglucosamine / chemistry*
Acetylglucosamine / metabolism*
Amino Acid Sequence
Animals
Epidermal Growth Factor / chemistry
Epidermal Growth Factor / metabolism
Extracellular Space / metabolism*
Humans
Protein Domains

Substances

Epidermal Growth Factor
Acetylglucosamine