ArticleBrain : a journal of neurology2020
Novel congenital disorder of O-linked glycosylation caused by GALNT2 loss of function.
Article in Brain : a journal of neurology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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53 citing papers in PubMed, 80 citations in OpenAlex.
- Integrated molecular mechanisms of salinity response in Apostichopus japonicus: focus on miRNA-driven core pathways and target gene regulation.Marine biotechnology (New York, N.Y.) · 2026Review
- Beyond the sugar coating: mucin-type O-Glycosylation as an underappreciated player in brain function and disease.Molecular psychiatry · 2026Review
- Molecular regulation and physiological role of GOLPH3-mediated Golgi retention.Nature communications · 2026Article
- Glycosylation disorders in pediatric epilepsy: pathophysiology, imaging and precision therapy.Frontiers in neurology · 2026Review
- Genome-wide association study of nutrient composition in meat from three two-way crossbred pig populations using whole-genome resequencing.Frontiers in veterinary science · 2026Article
- Interferon-stimulated gene GALNT2 restricts respiratory virus infections.Nature microbiology · 2026Article
- Review
- Decoding the complex substrate specificities of GalNAc-Ts.Glycobiology · 2025Review
- Complex de novo structural variants are an underestimated cause of rare disorders.Nature communications · 2025Article
- Neuromuscular Defects in aBiomolecules · 2025Article
- Article
- The glycoprotein quality control factor Malectin promotes coronavirus replication and viral protein biogenesis.bioRxiv : the preprint server for biology · 2025Article
- Midline assembloids reveal regulators of human axon guidance.Science (New York, N.Y.) · 2025Article
- O-GalNAc glycans are enriched in neuronal tracts and regulate nodes of Ranvier.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Glycosylation Pathways Targeted by Deregulated miRNAs in Autism Spectrum Disorder.International journal of molecular sciences · 2025Article
- Mass Spectrometry as a First-Line Diagnostic Aid for Congenital Disorders of Glycosylation.Mass spectrometry (Tokyo, Japan) · 2025Review
- Analysis of variant interactions in families with autism points to genes involved in the development of the central nervous system.PloS one · 2025Article
- Dynamic glycosylation remodeling in neurological disorders.Frontiers in molecular neuroscience · 2025Review
- Article
- Rational Design of Dual-Domain Binding Inhibitors forJACS Au · 2024Article
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Authors and funding
32 authors at 16 institutions in 6 countries.
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Abstract
Congenital disorders of glycosylation are a growing group of rare genetic disorders caused by deficient protein and lipid glycosylation. Here, we report the clinical, biochemical, and molecular features of seven patients from four families with GALNT2-congenital disorder of glycosylation (GALNT2-CDG), an O-linked glycosylation disorder. GALNT2 encodes the Golgi-localized polypeptide N-acetyl-d-galactosamine-transferase 2 isoenzyme. GALNT2 is widely expressed in most cell types and directs initiation of mucin-type protein O-glycosylation. All patients showed loss of O-glycosylation of apolipoprotein C-III, a non-redundant substrate for GALNT2. Patients with GALNT2-CDG generally exhibit a syndrome characterized by global developmental delay, intellectual disability with language deficit, autistic features, behavioural abnormalities, epilepsy, chronic insomnia, white matter changes on brain MRI, dysmorphic features, decreased stature, and decreased high density lipoprotein cholesterol levels. Rodent (mouse and rat) models of GALNT2-CDG recapitulated much of the human phenotype, including poor growth and neurodevelopmental abnormalities. In behavioural studies, GALNT2-CDG mice demonstrated cerebellar motor deficits, decreased sociability, and impaired sensory integration and processing. The multisystem nature of phenotypes in patients and rodent models of GALNT2-CDG suggest that there are multiple non-redundant protein substrates of GALNT2 in various tissues, including brain, which are critical to normal growth and development.
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