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Requirement for a core 1 galactosyltransferase in the Drosophila nervous system
Author(s) -
Lin YuhRu,
Reddy B.V.V.G.,
Irvine Kenneth D.
Publication year - 2008
Publication title -
developmental dynamics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.634
H-Index - 141
eISSN - 1097-0177
pISSN - 1058-8388
DOI - 10.1002/dvdy.21775
Subject(s) - biology , glycosylation , mucin , microbiology and biotechnology , axon guidance , mutant , nervous system , galactosyltransferase , genetics , phenotype , gene , biochemistry , axon , neuroscience , enzyme
Abstract Mucin type O ‐glycosylation is a widespread modification of eukaryotic proteins, but its functional requirements remain incompletely understood. It is initiated by the attachment of N‐acetylgalactosamine (GalNAc) to Ser or Thr residues, and then elongated by additional sugars. We have examined requirements for mucin‐type glycosylation in Drosophila by characterizing the expression and phenotypes of core 1 galactosyltransferases (core 1 GalTs), which elongate O ‐GalNAc by adding galactose in a β1,3 linkage. Drosophila encode several putative core 1 GalTs, each expressed in distinct patterns. CG9520 ( C1GalTA ) is expressed in the amnioserosa and central nervous system. A null mutation in C1GalTA is lethal, and mutant animals exhibit a striking morphogenetic defect in which the ventral nerve cord is greatly elongated and the brain hemispheres are misshapen. Lectin staining and blotting experiments confirmed that C1GalTA contributes to the synthesis of Gal‐β1,3‐GalNAc in vivo. Our results identify a role for mucin‐type O ‐glycosylation during neural development in Drosophila . Developmental Dynamics 237:3703–3714, 2008. © 2008 Wiley‐Liss, Inc.