mummy encodes an UDP- N-acetylglucosamine-dipohosphorylase and is required during Drosophila dorsal closure and nervous system development

Throughout development cell–cell interactions are of pivotal importance. Cells bind to each other or share information via secreted signaling molecules. To a large degree, these processes are modulated by post-translational modifications of membrane proteins. Glycan-chains are frequently added to me...

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Bibliographic Details
Published in:Mechanisms of development 2006-06, Vol.123 (6), p.487-499
Main Authors: Schimmelpfeng, Kristina, Strunk, Mareike, Stork, Tobias, Klämbt, Christian
Format: Article
Language:English
Subjects:
Animals
Axon patterning
Axons - metabolism
Body Patterning
Dorsal closure
Drosophila
Drosophila melanogaster - metabolism
Drosophila Proteins - metabolism
Eye - embryology
Gene Expression Regulation, Developmental
Glycosylation
Lectins - chemistry
Models, Genetic
Mutation
Nervous System - embryology
Nucleotidyltransferases - genetics
Nucleotidyltransferases - metabolism
Nucleotidyltransferases - physiology
Phosphorylation
UDP- N-acetylglucosamine-diphosphorylase
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Summary:Throughout development cell–cell interactions are of pivotal importance. Cells bind to each other or share information via secreted signaling molecules. To a large degree, these processes are modulated by post-translational modifications of membrane proteins. Glycan-chains are frequently added to membrane proteins and assist their exact function at the cell surface. In addition, the glycosylation pathway is required to generate GPI-linkage in the endoplasmatic reticulum. Here, we describe the analysis of the cabrio/ mummy gene, which encodes an UDP- N-acetylglucosamine diphosphorylase. This is a well-conserved and central enzyme in the glycosylation pathway. As expected from this central role in glycosylation, cabrio/ mummy mutants show many phenotypic traits ranging from CNS fasciculation defects to defects in dorsal closure and eye development. These phenotypes correlate well with specific glycosylation and GPI-anchorage defects in mummy mutants.
ISSN:0925-4773
1872-6356
DOI:10.1016/j.mod.2006.03.004