ArticleThe Journal of biological chemistry2012
Multiple members of the UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase family are essential for viability in Drosophila.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed.
- An in vivo chemical genetic approach for targeted glycoproteome analysis inbioRxiv : the preprint server for biology · 2026Article
- Synthesis of Polyhydroxylated Pyrrolidinyl Analogs of Sugar Nucleotides. Experimental and Computational Studies on Their Interactions With GalNAC-T's.Chembiochem : a European journal of chemical biology · 2026Article
- Genomic Signatures of Microgeographic Adaptation in Anopheles coluzzii Across Urban, Rural, and Forested Environments in Gabon.Molecular ecology · 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
- Article
- Regionalization of gene expression and cell types in the silk gland of the pantry mothbioRxiv : the preprint server for biology · 2025Article
- Divergent Genetic Pathways Underlying Convergent Parasitic Behaviours in Blowflies.Molecular ecology · 2025Article
- Advances in protein glycosylation and its role in tissue repair and regeneration.Glycoconjugate journal · 2023Review
- JiangShi(): a widely distributed Mucin-like protein essential for Drosophila development.G3 (Bethesda, Md.) · 2022Article
- In vivo models of mucin biosynthesis and function.Advanced drug delivery reviews · 2022Review
- Identification of GOLPH3 Partners inCells · 2021Article
- Asparaginyl endopeptidases: enzymology, applications and limitations.Organic & biomolecular chemistry · 2021Review
- Mucin-Type O-GalNAc Glycosylation in Health and Disease.Advances in experimental medicine and biology · 2021Article
- RNAi-Mediated Silencing of Pgants Shows Core 1Frontiers in physiology · 2021Article
- Multi-level analysis of reproduction in an Antarctic midge identifies female and male accessory gland products that are altered by larval stress and impact progeny viability.Scientific reports · 2020Article
- Ser and Thr acceptor preferences of the GalNAc-Ts vary among isoenzymes to modulate mucin-type O-glycosylation.Glycobiology · 2020Article
- Differential splicing of the lectin domain of anThe Journal of biological chemistry · 2020Article
- Synthesis and biological roles of O-glycans in insects.Glycoconjugate journal · 2020Review
- Functional analysis of glycosylation using Drosophila melanogaster.Glycoconjugate journal · 2020Review
- Loss of the disease-associated glycosyltransferase Galnt3 alters Muc10 glycosylation and the composition of the oral microbiome.The Journal of biological chemistry · 2020Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Mucin-type O-glycosylation represents a major form of post-translational modification that is conserved across most eukaryotic species. This type of glycosylation is initiated by a family of enzymes (GalNAc-Ts in mammals and PGANTs in Drosophila) whose members are expressed in distinct spatial and temporal patterns during development. Previous work from our group demonstrated that one member of this family is essential for viability and another member modulates extracellular matrix composition and integrin-mediated cell adhesion during development. To investigate whether other members of this family are essential, we employed RNA interference (RNAi) to each gene in vivo. Using this approach, we identified 4 additional pgant genes that are required for viability. Ubiquitous RNAi to pgant4, pgant5, pgant7, or the putative glycosyltransferase CG30463 resulted in lethality. Tissue-specific RNAi was also used to define the specific organ systems and tissues in which each essential family member is required. Interestingly, each essential pgant had a unique complement of tissues in which it was required. Additionally, certain tissues (mesoderm, digestive system, and tracheal system) required more than one pgant, suggesting unique functions for specific enzymes in these tissues. Expanding upon our RNAi results, we found that conventional mutations in pgant5 resulted in lethality and specific defects in specialized cells of the digestive tract, resulting in loss of proper digestive system acidification. In summary, our results highlight essential roles for O-glycosylation and specific members of the pgant family in many aspects of development and organogenesis.
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