ArticleThe Journal of biological chemistry2016
Multiple Domains of GlcNAc-1-phosphotransferase Mediate Recognition of Lysosomal Enzymes.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 48 citations in OpenAlex.
- Molecular insights into the regulation of GNPTαβ by LYSET.Nature communications · 2026Article
- Disruption of Man-6-P-Dependent Sorting to Lysosomes Confers IGF1R-Mediated Apoptosis Resistance.International journal of molecular sciences · 2025Article
- LYSET facilitates integration of both the N- and C-terminal transmembrane helices/cytoplasmic domains of GlcNAc-1-phosphotransferase.Molecular biology of the cell · 2025Article
- Article
- Multi-omic analysis of a mucolipidosis II neuronal cell model uncovers involvement of pathways related to neurodegeneration and drug metabolism.Molecular genetics and metabolism · 2024Article
- Elucidating the cellular determinants of targeted membrane protein degradation by lysosome-targeting chimeras.Science (New York, N.Y.) · 2023Article
- Multiplex tandem mass spectrometry enzymatic activity assay for the screening and diagnosis of Mucolipidosis type II and III.Molecular genetics and metabolism reports · 2023Article
- Structures of the mannose-6-phosphate pathway enzyme, GlcNAc-1-phosphotransferase.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structure of the human GlcNAc-1-phosphotransferase αβ subunits reveals regulatory mechanism for lysosomal enzyme glycan phosphorylation.Nature structural & molecular biology · 2022Article
- Elevated mRNA expression and defective processing of cathepsin D in HeLa cells lacking the mannose 6-phosphate pathway.FEBS open bio · 2021Article
- Differential recognition of oligomannose isomers by glycan-binding proteins involved in innate and adaptive immunity.Science advances · 2021Article
- Inactivation of the three GGA genes in HeLa cells partially compromises lysosomal enzyme sorting.FEBS open bio · 2021Article
- Clinical, radiological and computational studies on two novel GNPTG variants causing mucolipidosis III gamma phenotypes with varying severity.Molecular biology reports · 2021Article
- In VitroJournal of microbiology and biotechnology · 2021Article
- Disease-causing missense mutations within the N-terminal transmembrane domain of GlcNAc-1-phosphotransferase impair endoplasmic reticulum translocation or Golgi retention.Human mutation · 2020Article
- Upregulation of Sortilin, a Lysosomal Sorting Receptor, Corresponds with Reduced Bioavailability of Latent TGFβ in Mucolipidosis II Cells.Biomolecules · 2020Article
- Cell-autonomous expression of the acid hydrolase galactocerebrosidase.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Toward Engineering the Mannose 6-Phosphate Elaboration Pathway in Plants for Enzyme Replacement Therapy of Lysosomal Storage Disorders.Journal of clinical medicine · 2019Article
- Replication of Coxiella burnetii in a Lysosome-Like Vacuole Does Not Require Lysosomal Hydrolases.Infection and immunity · 2019Article
- "Stuck on sugars - how carbohydrates regulate cell adhesion, recognition, and signaling".Glycoconjugate journal · 2019Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The Golgi enzyme UDP-GlcNAc:lysosomal enzymeN-acetylglucosamine-1-phosphotransferase (GlcNAc-1-phosphotransferase), an α2β2γ2hexamer, mediates the initial step in the addition of the mannose 6-phosphate targeting signal on newly synthesized lysosomal enzymes. This tag serves to direct the lysosomal enzymes to lysosomes. A key property of GlcNAc-1-phosphotransferase is its unique ability to distinguish the 60 or so lysosomal enzymes from the numerous non-lysosomal glycoproteins with identical Asn-linked glycans. In this study, we demonstrate that the two Notch repeat modules and the DNA methyltransferase-associated protein interaction domain of the α subunit are key components of this recognition process. Importantly, different combinations of these domains are involved in binding to individual lysosomal enzymes. This study also identifies the γ-binding site on the α subunit and demonstrates that in the majority of instances the mannose 6-phosphate receptor homology domain of the γ subunit is required for optimal phosphorylation. These findings serve to explain how GlcNAc-1-phosphotransferase recognizes a large number of proteins that lack a common structural motif.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.