Dystroglycan and protein O-mannosyltransferases 1 and 2 are required to maintain integrity of Drosophila larval muscles

In vertebrates, mutations in Protein O-mannosyltransferase1 (POMT1) or POMT2 are associated with muscular dystrophy due to a requirement for O-linked mannose glycans on the Dystroglycan (Dg) protein. In this study we examine larval body wall muscles of Drosophila mutant for Dg, or RNA interference k...

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Bibliographic Details
Published in:Molecular biology of the cell 2007-12, Vol.18 (12), p.4721-4730
Main Authors: Haines, Nicola, Seabrooke, Sara, Stewart, Bryan A
Format: Article
Language:English
Subjects:
Animals
Drosophila melanogaster - genetics
Drosophila melanogaster - growth & development
Drosophila melanogaster - metabolism
Dystroglycans - genetics
Dystroglycans - metabolism
Electrophysiology
Gene Expression Regulation, Developmental
Laminin - metabolism
Larva - genetics
Larva - metabolism
Mannosyltransferases - genetics
Mannosyltransferases - metabolism
Muscles - abnormalities
Muscles - metabolism
Mutation - genetics
RNA Interference
Sarcomeres - metabolism
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Summary:In vertebrates, mutations in Protein O-mannosyltransferase1 (POMT1) or POMT2 are associated with muscular dystrophy due to a requirement for O-linked mannose glycans on the Dystroglycan (Dg) protein. In this study we examine larval body wall muscles of Drosophila mutant for Dg, or RNA interference knockdown for Dg and find defects in muscle attachment, altered muscle contraction, and a change in muscle membrane resistance. To determine if POMTs are required for Dg function in Drosophila, we examine larvae mutant for genes encoding POMT1 or POMT2. Larvae mutant for either POMT, or doubly mutant for both, show muscle attachment and muscle contraction phenotypes identical to those associated with reduced Dg function, consistent with a requirement for O-linked mannose on Drosophila Dg. Together these data establish a central role for Dg in maintaining integrity in Drosophila larval muscles and demonstrate the importance of glycosylation to Dg function in Drosophila. This study opens the possibility of using Drosophila to investigate muscular dystrophy.
ISSN:1059-1524
1939-4586
DOI:10.1091/mbc.E07-01-0047