ArticleProceedings of the National Academy of Sciences of the United States of America2014
Mislocalization of phosphotransferase as a cause of mucolipidosis III αβ.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 26 citations in OpenAlex.
- Molecular insights into the regulation of GNPTαβ by LYSET.Nature communications · 2026Article
- LYSET facilitates integration of both the N- and C-terminal transmembrane helices/cytoplasmic domains of GlcNAc-1-phosphotransferase.Molecular biology of the cell · 2025Article
- The human disease gene LYSET is essential for lysosomal enzyme transport and viral infection.Science (New York, N.Y.) · 2022Article
- Pathogenic variants in GNPTAB and GNPTG encoding distinct subunits of GlcNAc-1-phosphotransferase differentially impact bone resorption in patients with mucolipidosis type II and III.Genetics in medicine : official journal of the American College of Medical Genetics · 2021Article
- Mucolipidoses Overview: Past, Present, and Future.International journal of molecular sciences · 2020Review
- Disease-causing missense mutations within the N-terminal transmembrane domain of GlcNAc-1-phosphotransferase impair endoplasmic reticulum translocation or Golgi retention.Human mutation · 2020Article
- Recycling of Golgi glycosyltransferases requires direct binding to coatomer.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- MammalianThe Journal of biological chemistry · 2017Article
- Mucolipidosis III GNPTG Missense Mutations Cause Misfolding of the γ Subunit of GlcNAc-1-Phosphotransferase.Human mutation · 2016Article
- Clec16a is Critical for Autolysosome Function and Purkinje Cell Survival.Scientific reports · 2016Article
- Tuberous sclerosis, polycystic kidney disease and mucolipidosis III gamma caused by a microdeletion unmasking a recessive mutation.American journal of medical genetics. Part A · 2015Article
- The lysosomal enzyme receptor protein (LERP) is not essential, but is implicated in lysosomal function in Drosophila melanogaster.Biology open · 2015Article
- Analyses of disease-related GNPTAB mutations define a novel GlcNAc-1-phosphotransferase interaction domain and an alternative site-1 protease cleavage site.Human molecular genetics · 2015Article
- Analysis of mucolipidosis II/III GNPTAB missense mutations identifies domains of UDP-GlcNAc:lysosomal enzyme GlcNAc-1-phosphotransferase involved in catalytic function and lysosomal enzyme recognition.The Journal of biological chemistry · 2015Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The lysosomal storage disorder mucolipidosis III αβ is caused by mutations in the αβ subunits of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase (phosphotransferase). This Golgi-localized enzyme mediates the first step in the synthesis of the mannose 6-phosphate recognition marker on lysosomal acid hydrolases, and loss of function results in impaired lysosomal targeting of these acid hydrolases and decreased lysosomal degradation. Here we show that two patient missense mutations, Lys4Gln and Ser15Tyr, in the N-terminal cytoplasmic tail of the α subunit of phosphotransferase impair retention of the catalytically active enzyme in the Golgi complex. This results in mistargeting of the mutant phosphotransferases to lysosomes, where they are degraded, or to the cell surface and release into the medium. The finding that mislocalization of active phosphotransferase is the basis for mucolipidosis III αβ in a subset of patients shows the importance of single residues in the cytoplasmic tail of a Golgi-resident protein for localization to this compartment.
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