ArticleGlycobiology2018
Members of the GalNAc-T family of enzymes utilize distinct Golgi localization mechanisms.
Article in Glycobiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 21 citations in OpenAlex.
- Cell autonomous inflammation in VEXAS is mediated by cGAS-STING.bioRxiv : the preprint server for biology · 2026Article
- Interaction with COPII Member SAR1 Is Critical for the Delivery ofPlants (Basel, Switzerland) · 2026Article
- Glycosylation in premature ovarian insufficiency: from genetic etiology to precision diagnostics.Journal of ovarian research · 2026Review
- Golgi Drivers of Cancer.Sub-cellular biochemistry · 2026Review
- Trafficking and localization of Golgi-residentFrontiers in plant science · 2025Review
- Pathogenesis of IgA nephropathy: Omics data inform glycomedicine.Nephrology (Carlton, Vic.) · 2024Article
- Protein nanobarcodes enable single-step multiplexed fluorescence imaging.PLoS biology · 2023Article
- Quantitative mapping of the in vivo O-GalNAc glycoproteome in mouse tissues identifies GalNAc-T2 O-glycosites in metabolic disorder.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- O-Linked Sialoglycans Modulate the Proteolysis of SARS-CoV-2 Spike and Likely Contribute to the Mutational Trajectory in Variants of Concern.ACS central science · 2023Article
- Polypeptide N-acetylgalactosamine transferase 3: a post-translational writer on human health.Journal of molecular medicine (Berlin, Germany) · 2022Review
- Article
- Critical Determinants in ER-Golgi Trafficking of Enzymes Involved in Glycosylation.Plants (Basel, Switzerland) · 2022Review
- Early-Stage Loss of GALNT6 Predicts Poor Clinical Outcome in Colorectal Cancer.Frontiers in oncology · 2022Article
- The Role of APPBiomolecules · 2020Review
- TheFrontiers in cell and developmental biology · 2019Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Mucin-type O-glycosylation is an evolutionarily conserved and essential post-translational protein modification that is initiated in the Golgi apparatus by a family of enzymes known as the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-Ts). GalNAc-Ts are type II membrane proteins which contain short N-terminal tails located in the cytoplasm, a transmembrane domain that crosses the Golgi membrane, to which is connected a stem region that tethers the C-terminal catalytic and lectin domains that reside in the Golgi lumen. Although mucin-type O-glycans have been shown to play critical roles in numerous biological processes, little is known about how the GalNAc-Ts are targeted to their site of action within the Golgi complex. Here, we investigate the essential protein domains required for Golgi localization of four representative members of the GalNAc-T family of enzymes. We find that GalNAc-T1 and -T2 require their cytoplasmic tail and transmembrane domains for proper Golgi localization, while GalNAc-T10 requires its transmembrane and luminal stem domains. GalNAc-T7 can use either its cytoplasmic tail or its luminal stem, in combination with its transmembrane domain, to localize to the Golgi. We determined that a single glutamic acid in the GalNAc-T10 cytoplasmic tail inhibits its ability to localize to the Golgi via a cytoplasmic tail-dependent mechanism. We therefore demonstrate that despite their similarity, different members of this enzyme family are directed to the Golgi by more than one set of targeting signals.
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