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J. Biol. Chem., Vol. 278, Issue 3, 1411-1414, January 17, 2003

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ACCELERATED PUBLICATION
Drosophila egghead Encodes a 1,4-Mannosyltransferase Predicted to Form the Immediate Precursor Glycosphingolipid Substrate for brainiac^*

Hans H. Wandall, Johannes W. Pedersen, Chaeho Park^§, Steven B. Levery^§, Sandrine Pizette^¶, Stephen M. Cohen^¶, Tilo Schwientek, and Henrik Clausen

From the  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, and the ^¶ European Molecular Biology Laboratory, Meyerhofstr 1, 69117 Heidelberg, Germany

The neurogenic Drosophila genes brainiac and egghead are essential for epithelial development in the embryo and in oogenesis. Analysis of egghead and brainiac mutants has led to the suggestion that the two genes function in a common signaling pathway. Recently, brainiac was shown to encode a UDP-N-acetylglucosamine:Man1,3-N-acetylglucosaminyltransferase (3GlcNAc-transferase) tentatively assigned a key role in biosynthesis of arthroseries glycosphingolipids and forming the trihexosylceramide, GlcNAc1-3Man1-4Glc1-1Cer. In the present study we demonstrate that egghead encodes a Golgi-located GDP-mannose:Glc1,4-mannosyltransferase tentatively assigned a biosynthetic role to form the precursor arthroseries glycosphingolipid substrate for Brainiac, Man1-4Glc1-1Cer. Egghead is unique among eukaryotic gly- cosyltransferase genes in that homologous genes are limited to invertebrates, which correlates with the exclusive existence of arthroseries glycolipids in invertebrates. We propose that brainiac and egghead function in a common biosynthetic pathway and that inactivating mutations in either lead to sufficiently early termination of glycolipid biosynthesis to inactivate essential functions mediated by glycosphingolipids.

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