An O-glycosyltransferase is required for proper salivary gland development in Drosophila

Monday, October 24, 2011 — Poster Session I
Noon – 2:00 p.m.	Natcher Conference Center	NIDCR	DEV-11

Authors

• D Tran
• K Ten Hagen

Abstract

Drosophila salivary glands are the largest secretory structures of the fly and represent a valuable system for the study of epithelial tube formation and organ morphogenesis. A major component of salivary gland secretions are heavily O-glycosylated proteins that serve diverse functions. Protein O-glycosylation is initiated by a family of enzymes (PGANTs in Drosophila) that catalyze the transfer of GalNAc to the hydroxyl group of either serine or threonine in protein substrates. There are 12 pgant genes in Drosophila that are expressed throughout development. Here we demonstrate that one of these glycosyltransferases (pgant5) is required for proper salivary gland development. Mutations in pgant5, as well as RNA interference (RNAi) to pgant5 resulted in small, irregularly shaped larval salivary glands. Reduced gland size in pgant5 mutants was due to a reduction in cell size rather than cell number. Additionally, mutant salivary glands also displayed irregular apical membranes and expanded lumens. Real-time PCR of mutant glands showed an increase in the transcript levels of the apical membrane determinant Crumbs. Our data suggests that pgant5 is required for proper apical membrane and lumen formation of the salivary glands. Future studies will focus on elucidating the specific mechanism of PGANT5 function in the salivary gland.

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