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Citation
Ji, S., Samara, N.L., Revoredo, L., Zhang, L., Tran, D.T., Muirhead, K., Tabak, L.A., Ten Hagen, K.G. (2018). A molecular switch orchestrates enzyme specificity and secretory granule morphology.  Nat. Commun. 9(1): 3508.
FlyBase ID
FBrf0239944
Publication Type
Research paper
Abstract
Regulated secretion is an essential process where molecules destined for export are directed to membranous secretory granules, where they undergo packaging and maturation. Here, we identify a gene (pgant9) that influences the structure and shape of secretory granules within the Drosophila salivary gland. Loss of pgant9, which encodes an O-glycosyltransferase, results in secretory granules with an irregular, shard-like morphology, and altered glycosylation of cargo. Interestingly, pgant9 undergoes a splicing event that acts as a molecular switch to alter the charge of a loop controlling access to the active site of the enzyme. The splice variant with the negatively charged loop glycosylates the positively charged secretory cargo and rescues secretory granule morphology. Our study highlights a mechanism for dictating substrate specificity within the O-glycosyltransferase enzyme family. Moreover, our in vitro and in vivo studies suggest that the glycosylation status of secretory cargo influences the morphology of maturing secretory granules.
PubMed ID
PubMed Central ID
PMC6115407 (PMC) (EuropePMC)
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    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    Nat. Commun.
    Title
    Nature communications
    ISBN/ISSN
    2041-1723
    Data From Reference
    Aberrations (1)
    Alleles (6)
    Genes (3)
    Physical Interactions (2)
    Cell Lines (1)
    Natural transposons (1)
    Insertions (3)
    Experimental Tools (2)
    Transgenic Constructs (3)