ArticleProceedings of the National Academy of Sciences of the United States of America2022
Structures of the mannose-6-phosphate pathway enzyme, GlcNAc-1-phosphotransferase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- M6PR/IGF2R double-knockout supplies therapeutic sources for mucolipidosis II and Niemann-Pick C2.The Journal of biological chemistry · 2026Article
- Relevance of functional studies for assessing an antisense oligonucleotide-mediated exon skipping therapeutic strategy for mucolipidosis type II.Orphanet journal of rare diseases · 2026Article
- Molecular insights into the regulation of GNPTαβ by LYSET.Nature communications · 2026Article
- Identification of potential biomarkers related to mannose metabolism in keloids: analysis of integrated bulk RNA-seq and scRNA-seq.Frontiers in immunology · 2026Article
- Autophagy-lysosomal pathway in neurodegeneration.Molecular neurodegeneration advances · 2026Review
- A stuttering-associatedbioRxiv : the preprint server for biology · 2025Article
- Effect of glycosylation on protein folding: From biological roles to chemical protein synthesis.iScience · 2025Review
- Clinical and molecular characteristics of 20 Chinese probands with Mucolipidosis type II and III alpha/beta.BMC pediatrics · 2024Article
- The host mannose-6-phosphate pathway and viral infection.Frontiers in cellular and infection microbiology · 2024Review
- Structural and Functional Insights into the Stealth Protein CpsY ofBiomolecules · 2023Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The mannose-6-phosphate (M6P) pathway is responsible for the transport of hydrolytic enzymes to lysosomes. N-acetylglucosamine-1-phosphotransferase (GNPT) catalyzes the first step of tagging these hydrolases with M6P, which when recognized by receptors in the Golgi diverts them to lysosomes. Genetic defects in the GNPT subunits, GNPTAB and GNPTG, cause the lysosomal storage diseases mucolipidosis types II and III. To better understand its function, we determined partial three-dimensional structures of the GNPT complex. The catalytic domain contains a deep cavity for binding of uridine diphosphate-
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