ArticleNature communications2018
A molecular switch orchestrates enzyme specificity and secretory granule morphology.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- An in vivo chemical genetic approach for targeted glycoproteome analysis inbioRxiv : the preprint server for biology · 2026Article
- A single catalytic domain residue regulates the substrate specificity of a mucin-type O-glycosyltransferase in salivary gland function.bioRxiv : the preprint server for biology · 2025Article
- Decoding the complex substrate specificities of GalNAc-Ts.Glycobiology · 2025Review
- Article
- The FAM114A proteins are adaptors for the recycling of Golgi enzymes.Journal of cell science · 2024Article
- O-Glycosylation of a male seminal fluid protein influences sperm binding and female postmating behavior.PNAS nexus · 2024Article
- A Toxoplasma gondii O-glycosyltransferase that modulates bradyzoite cyst wall rigidity is distinct from host homologues.Nature communications · 2024Article
- A novel cysteine-rich adaptor protein is required for mucin packaging and secretory granule stability in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Functional evaluation of novel variants ofFrontiers in neuroscience · 2024Article
- Transcriptional changes in specific subsets of Drosophila neurons following inhibition of the serotonin transporter.Translational psychiatry · 2023Article
- Bump-and-hole engineering of human polypeptide N-acetylgalactosamine transferases to dissect their protein substrates and glycosylation sites in cells.STAR protocols · 2023Article
- Transcriptional changes in specific subsets of Drosophila neurons following inhibition of the serotonin transporter.Research square · 2023Article
- In vivo characterization of Drosophila golgins reveals redundancy and plasticity of vesicle capture at the Golgi apparatus.Current biology : CB · 2022Article
- Regulated Restructuring of Mucins During Secretory Granule Maturation In Vivo.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Drosophila Glue: A Promising Model for Bioadhesion.Insects · 2022Review
- In vivo models of mucin biosynthesis and function.Advanced drug delivery reviews · 2022Review
- Structural and mechanistic investigations of protein S-glycosyltransferases.Cell chemical biology · 2021Article
- Furin cleavage of the SARS-CoV-2 spike is modulated byProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Furin cleavage of the SARS-CoV-2 spike is modulated by O-glycosylation.bioRxiv : the preprint server for biology · 2021Article
- Ser and Thr acceptor preferences of the GalNAc-Ts vary among isoenzymes to modulate mucin-type O-glycosylation.Glycobiology · 2020Article
Corrections and comments
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Authors and funding
8 authors.
Funding
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.
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