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Originally published In Press as doi:10.1074/jbc.M206213200 on July 18, 2002

J. Biol. Chem., Vol. 277, Issue 36, 32421-32429, September 6, 2002
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The Drosophila Gene brainiac Encodes a Glycosyltransferase Putatively Involved in Glycosphingolipid Synthesis*

Tilo SchwientekDagger §, Birgit KeckDagger §, Steven B. Levery||, Mads A. JensenDagger , Johannes W. PedersenDagger , Hans H. WandallDagger , Mark Stroud**, Stephen M. CohenDagger Dagger , Margarida AmadoDagger §§, and Henrik ClausenDagger ¶¶

From the Dagger  School of Dentistry, University of Copenhagen, Nørre Allé 20, 2200 Copenhagen N, Denmark, the || Department of Chemistry, University of New Hampshire, Durham, New Hampshire 03824, the ** Northwest Biotherapeutics, Inc., Bothell, Washington 98021, and the Dagger Dagger  European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany

The Drosophila genes fringe and brainiac exhibit sequence similarities to glycosyltransferases. Drosophila and mammalian fringe homologs encode UDP-N-acetylglucosamine:fucose-O-Ser beta 1,3-N-acetylglucosaminyltransferases that modulate the function of Notch family receptors. The biological function of brainiac is less well understood. brainiac is a member of a large homologous mammalian beta 3-glycosyltransferase family with diverse functions. Eleven distinct mammalian homologs have been demonstrated to encode functional enzymes forming beta 1-3 glycosidic linkages with different UDP donor sugars and acceptor sugars. The putative mammalian homologs with highest sequence similarity to brainiac encode UDP-N-acetylglucosamine:beta 1,3-N-acetylglucosaminyltransferases (beta 3GlcNAc-transferases), and in the present study we show that brainiac also encodes a beta 3GlcNAc-transferase that uses beta -linked mannose as well as beta -linked galactose as acceptor sugars. The inner disaccharide core structures of glycosphingolipids in mammals (Galbeta 1-4Glcbeta 1-Cer) and insects (Manbeta 1-4Glcbeta 1-Cer) are different. Both disaccharide glycolipids served as substrates for brainiac, but glycolipids of insect cells have so far only been found to be based on the GlcNAcbeta 1-3Manbeta 1-4Glcbeta 1-Cer core structure. Infection of High FiveTM cells with baculovirus containing full coding brainiac cDNA markedly increased the ratio of GlcNAcbeta 1-3Manbeta 1-4Glcbeta 1-Cer glycolipids compared with Galbeta 1-4Manbeta 1-4Glcbeta 1-Cer found in wild type cells. We suggest that brainiac exerts its biological functions by regulating biosynthesis of glycosphingolipids.

* This work was supported by The Danish Cancer Society, the Velux Foundation, the Danish Medical Research Council, the Lundbeck Foundation, the National Institutes of Health Resource Center for Biomedical Complex Carbohydrates (NIH P41 RR05351), and Biological Research Infrastructure Network-Center for Structural Biology (NIH P20 RR16459).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ These authors contributed equally and should be considered joint first authors.

Present address: Inst. of Biochemistry II, University of Cologne, Joseph-Stelzmann-Str. 52, 50931 Köln, Germany.

§§ Present address: Dept. of Molecular Biology, MEM-L71, The Scripps Research Inst., 10550 North Torrey Pines Rd., La Jolla, CA 92037.

¶¶ To whom correspondence should be addressed: School of Dentistry, Nørre Alle 20, DK-2200 Copenhagen N, Denmark. Tel.: 45-35326835; Fax: 45-35326505; E-mail: henrik.clausen@odont.ku.dk.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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