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Mucolipidosis II is caused by mutations in GNPTA encoding the alpha/beta GlcNAc-1-phosphotransferase

Standard

Mucolipidosis II is caused by mutations in GNPTA encoding the alpha/beta GlcNAc-1-phosphotransferase. / Tiede, Stephan; Storch, Stephan; Lübke, Torben; Henrissat, Bernard; Bargal, Ruth; Raas-Rothschild, Annick; Braulke, Thomas.

in: NAT MED, Jahrgang 11, Nr. 10, 01.10.2005, S. 1109-12.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Tiede, S, Storch, S, Lübke, T, Henrissat, B, Bargal, R, Raas-Rothschild, A & Braulke, T 2005, 'Mucolipidosis II is caused by mutations in GNPTA encoding the alpha/beta GlcNAc-1-phosphotransferase', NAT MED, Jg. 11, Nr. 10, S. 1109-12. https://doi.org/10.1038/nm1305

APA

Tiede, S., Storch, S., Lübke, T., Henrissat, B., Bargal, R., Raas-Rothschild, A., & Braulke, T. (2005). Mucolipidosis II is caused by mutations in GNPTA encoding the alpha/beta GlcNAc-1-phosphotransferase. NAT MED, 11(10), 1109-12. https://doi.org/10.1038/nm1305

Vancouver

Tiede S, Storch S, Lübke T, Henrissat B, Bargal R, Raas-Rothschild A et al. Mucolipidosis II is caused by mutations in GNPTA encoding the alpha/beta GlcNAc-1-phosphotransferase. NAT MED. 2005 Okt 1;11(10):1109-12. https://doi.org/10.1038/nm1305

Bibtex

@article{39ff78b871184052948830359a7ef8c4,
title = "Mucolipidosis II is caused by mutations in GNPTA encoding the alpha/beta GlcNAc-1-phosphotransferase",
abstract = "Mucolipidosis II (ML II) is a fatal lysosomal storage disorder resulting from defects in the multimeric GlcNAc-1-phosphotransferase responsible for the initial step in the generation of the mannose 6-phosphate (M6P) recognition marker. M6P residues on oligosaccharides of newly synthesized lysosomal enzymes are essential for efficient receptor-mediated transport to lysosomes. We used the recombinant GlcNAc-1-phosphotransferase gamma subunit as an affinity matrix to purify an unknown protein identified as the product of GNPTA (encoding GNPTA, previously known as MGC4170). The cDNA encodes a protein of 1,256 amino acids with two putative transmembrane domains and a complex preserved modular structure comprising at least six domains. The N-terminal domain of GNPTA, interrupted by a long insertion, shows similarities to bacterial capsule biosynthesis proteins. We identified seven mutations in GNPTA that lead to premature translational termination in six individuals with ML II. Retroviral transduction of fibroblasts from an individual with ML II resulted in the expression and localization of GNPTA in the Golgi apparatus, accompanied by the correction of hypersecretion of lysosomal enzymes. Our results provide evidence that GNPTA encodes a subunit of GlcNAc-1-phosphotransferase defective in individuals with ML II.",
keywords = "Amino Acid Sequence, Fibroblasts, Humans, Molecular Sequence Data, Mucolipidoses, Mutation, Sequence Homology, Amino Acid, Transferases (Other Substituted Phosphate Groups)",
author = "Stephan Tiede and Stephan Storch and Torben L{\"u}bke and Bernard Henrissat and Ruth Bargal and Annick Raas-Rothschild and Thomas Braulke",
year = "2005",
month = oct,
day = "1",
doi = "10.1038/nm1305",
language = "English",
volume = "11",
pages = "1109--12",
journal = "NAT MED",
issn = "1078-8956",
publisher = "NATURE PUBLISHING GROUP",
number = "10",

}

RIS

TY - JOUR

T1 - Mucolipidosis II is caused by mutations in GNPTA encoding the alpha/beta GlcNAc-1-phosphotransferase

AU - Tiede, Stephan

AU - Storch, Stephan

AU - Lübke, Torben

AU - Henrissat, Bernard

AU - Bargal, Ruth

AU - Raas-Rothschild, Annick

AU - Braulke, Thomas

PY - 2005/10/1

Y1 - 2005/10/1

N2 - Mucolipidosis II (ML II) is a fatal lysosomal storage disorder resulting from defects in the multimeric GlcNAc-1-phosphotransferase responsible for the initial step in the generation of the mannose 6-phosphate (M6P) recognition marker. M6P residues on oligosaccharides of newly synthesized lysosomal enzymes are essential for efficient receptor-mediated transport to lysosomes. We used the recombinant GlcNAc-1-phosphotransferase gamma subunit as an affinity matrix to purify an unknown protein identified as the product of GNPTA (encoding GNPTA, previously known as MGC4170). The cDNA encodes a protein of 1,256 amino acids with two putative transmembrane domains and a complex preserved modular structure comprising at least six domains. The N-terminal domain of GNPTA, interrupted by a long insertion, shows similarities to bacterial capsule biosynthesis proteins. We identified seven mutations in GNPTA that lead to premature translational termination in six individuals with ML II. Retroviral transduction of fibroblasts from an individual with ML II resulted in the expression and localization of GNPTA in the Golgi apparatus, accompanied by the correction of hypersecretion of lysosomal enzymes. Our results provide evidence that GNPTA encodes a subunit of GlcNAc-1-phosphotransferase defective in individuals with ML II.

AB - Mucolipidosis II (ML II) is a fatal lysosomal storage disorder resulting from defects in the multimeric GlcNAc-1-phosphotransferase responsible for the initial step in the generation of the mannose 6-phosphate (M6P) recognition marker. M6P residues on oligosaccharides of newly synthesized lysosomal enzymes are essential for efficient receptor-mediated transport to lysosomes. We used the recombinant GlcNAc-1-phosphotransferase gamma subunit as an affinity matrix to purify an unknown protein identified as the product of GNPTA (encoding GNPTA, previously known as MGC4170). The cDNA encodes a protein of 1,256 amino acids with two putative transmembrane domains and a complex preserved modular structure comprising at least six domains. The N-terminal domain of GNPTA, interrupted by a long insertion, shows similarities to bacterial capsule biosynthesis proteins. We identified seven mutations in GNPTA that lead to premature translational termination in six individuals with ML II. Retroviral transduction of fibroblasts from an individual with ML II resulted in the expression and localization of GNPTA in the Golgi apparatus, accompanied by the correction of hypersecretion of lysosomal enzymes. Our results provide evidence that GNPTA encodes a subunit of GlcNAc-1-phosphotransferase defective in individuals with ML II.

KW - Amino Acid Sequence

KW - Fibroblasts

KW - Humans

KW - Molecular Sequence Data

KW - Mucolipidoses

KW - Mutation

KW - Sequence Homology, Amino Acid

KW - Transferases (Other Substituted Phosphate Groups)

U2 - 10.1038/nm1305

DO - 10.1038/nm1305

M3 - SCORING: Journal article

C2 - 16200072

VL - 11

SP - 1109

EP - 1112

JO - NAT MED

JF - NAT MED

SN - 1078-8956

IS - 10

ER -