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Journal of Biochemistry Advance Access published online on February 13, 2008
Journal of Biochemistry, doi:10.1093/jb/mvn016
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© 2008 The Japanese Biochemical Society

JB Minireview

Biological functions of glycosyltransferase genes involved in O-fucose glycan synthesis

Tetsuya Okajima#, Aiko Matsuura and Tsukasa Matsuda

Nagoya University Graduate School of Bioagricultural Sciences, Department of Applied Molecular Biosciences, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan.

#To whom correspondence should be addressed: Dr. Tetsuya Okajima: TEL: 81-52-789-4131, Fax: 81-52-789-4128, Email: tokajima{at}arg.nagoya-u.ac.jp

Received December 3, 2007; Accepted January 11, 2008


  Abstract

Rare types of glycosylation often occur in a domain-specific manner and are involved in specific biological processes. Well-known examples of such modification are O-fucose and O-glucose glycans on epidermal growth factor (EGF) domains. In particular, O-fucose glycans are reported to regulate the functions of EGF domain-containing proteins such as urinary-type plasminogen activator and Notch receptors. Two glycosyltransferases catalyze the initiation and elongation of O-fucose glycans. The initiation process is catalyzed by O-fucosyltransferase 1, which is essential for Notch signaling in both Drosophila and mice. O-fucosyltransferase 1 can affect the folding, ligand interaction, and endocytosis of Notch receptors, and both the glycosyltransferase and non-catalytic activities of O-fucosyltransferase 1 have been reported. The elongation of O-fucose monosaccharide is catalyzed by fringe-related genes, which differentially modulate the interaction between Notch and 2 classes of ligands, namely, Delta and Serrate/Jagged. In this article, we have reviewed the recent reports addressing the distinctive features of the glycosyltransferases and O-glycans present on the EGF domains.

Key Words: Fringe, Notch, O-fucose, O-fucosyltransferase, O-glucose


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A. Matsuura, M. Ito, Y. Sakaidani, T. Kondo, K. Murakami, K. Furukawa, D. Nadano, T. Matsuda, and T. Okajima
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[Abstract] [Full Text] [PDF]


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