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The role of N‐Linked glycosylation during Drosophila development
Author(s) -
McCague Allison,
Selva Erica M.
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.594.4
Subject(s) - endoplasmic reticulum , glycosylation , microbiology and biotechnology , axon , axon guidance , biology , glycoprotein , mutant , drosophila (subgenus) , neuroscience , genetics , gene
N‐linked glycosylation is a key post‐translational modification for many secretory pathway targeted proteins. Endoplasmic reticulum glycosyltranferases construct a 14‐sugar precursor on a dolichol carrier, which is transferred to protein consensus sites. alg9 and alg10 N‐glycosylation mutants were used to examine the role of this modification during Drosophila development. alg10 encodes the enzyme catalyzing terminal glucose addition to the sugar‐precursor prior to transfer, while alg9 encodes an enzyme acting five steps earlier. In embryos, loss of alg9 and alg10 caused severe and pleotrophic defects. Central nervous system (CNS) neurons were specified in both alg9 and alg10 embryos. alg10 loss disrupted axon pathfinding, while alg9 embryos lacked mature neurons. Drosophila eye development in the absence of alg9 and alg10 yielded small rough adult eyes, but alg9 eyes were more severe. Examination of molecular markers in alg9 and alg10 late 3 rd instar eye imaginal discs suggested adult small rough adult eyes might be due to neuronal apoptosis. These eye discs also showed defects in axon pathfinding, as shown by the loss of Bolwig's nerve and disrupted axon tracks. These results suggest loss of alg10 may disrupt the maturation of a subset of N‐glycoproteins, since alg9, which acts earlier, has more severe developmental defects. Funding sources: UD Undergrad Research Program, NSF and HHMI