Rapid Publication Missense Mutations in N-Acetylglucosamine-1- Phosphotransferase a/b Subunit Gene in a Patient With Mucolipidosis III and a Mild Clinical Phenotype
نویسندگان
چکیده
Rapid Publication Missense Mutations in N-Acetylglucosamine-1Phosphotransferase a/b Subunit Gene in a Patient With Mucolipidosis III and a Mild Clinical Phenotype Stephan Tiede, Nicole Muschol, Gert Reutter, Michael Cantz, Kurt Ullrich, and Thomas Braulke* Department of Biochemistry, Children’s Hospital, University Hospital Hamburg Eppendorf, Hamburg, Germany Department of Rheumatology, Children’s Hospital, South Hospital, Nürnberg, Germany Institute of Pathochemistry and Neurochemistry, University of Heidelberg, Heidelberg, Germany
منابع مشابه
Mislocalization of phosphotransferase as a cause of mucolipidosis III αβ.
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 ...
متن کاملExome sequencing for mucolipidosis III: Detection of a novel GNPTAB gene mutation in a patient with a very mild phenotype
Mucolipidosis II and III alpha/beta (ML II/III alpha/beta) are rare autosomal recessive lysosomal storage diseases that are caused by a deficiency of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase, the enzyme responsible for the synthesis of the mannose 6-phosphate targeting signal on lysosomal hydrolases. A Brazilian patient suspected of having a very mild ML III was inve...
متن کاملMolecular basis of variant pseudo-hurler polydystrophy (mucolipidosis IIIC)
Mucolipidosis IIIC, or variant pseudo-Hurler polydystrophy, is an autosomal recessive disease of lysosomal hydrolase trafficking. Unlike the related diseases, mucolipidosis II and IIIA, the enzyme affected in mucolipidosis IIIC (N-Acetylglucosamine-1-phosphotransferase [GlcNAc-phosphotransferase]) retains full transferase activity on synthetic substrates but lacks activity on lysosomal hydrolas...
متن کاملAnalyses of disease-related GNPTAB mutations define a novel GlcNAc-1-phosphotransferase interaction domain and an alternative site-1 protease cleavage site
Mucolipidosis II (MLII) and III alpha/beta are autosomal-recessive diseases of childhood caused by mutations in GNPTAB encoding the α/β-subunit precursor protein of the GlcNAc-1-phosphotransferase complex. This enzyme modifies lysosomal hydrolases with mannose 6-phosphate targeting signals. Upon arrival in the Golgi apparatus, the newly synthesized α/β-subunit precursor is catalytically activat...
متن کاملONLINE MUTATION REPORT Genomic organisation of the UDP-N-acetylglucosamine-1- phosphotransferase gamma subunit (GNPTAG) and its mutations in mucolipidosis III
A Raas-Rothschild, R Bargal, O Goldman, E Ben-Asher, J E M Groener, A Toutain, E Stemmer, Z Ben-Neriah, H Flusser, F A Beemer, M Penttinen, T Olender, A J J T Rein, G Bach, M Zeigler . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . ...
متن کامل