ArticleThe Biochemical journal2011
Biochemical correlation of activity of the α-dystroglycan-modifying glycosyltransferase POMGnT1 with mutations in muscle-eye-brain disease.
Article in The Biochemical journal, 2011. 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, 19 citations in OpenAlex.
- Crystal structures of β-1,4-N-acetylglucosaminyltransferase 2: structural basis for inherited muscular dystrophies.Acta crystallographica. Section D, Structural biology · 2021Article
- Multifaceted antibodies development against synthetic α-dystroglycan mucin glycopeptide as promising tools for dystroglycanopathies diagnostic.Glycoconjugate journal · 2020Article
- ProteinThe Journal of biological chemistry · 2017Article
- Mutations in POMGNT1 cause non-syndromic retinitis pigmentosa.Human molecular genetics · 2016Article
- Expression pattern in retinal photoreceptors of POMGnT1, a protein involved in muscle-eye-brain disease.Molecular vision · 2016Article
- Matriglycan: a novel polysaccharide that links dystroglycan to the basement membrane.Glycobiology · 2015Review
- Golgi phosphoprotein 3 mediates the Golgi localization and function of protein O-linked mannose β-1,2-N-acetlyglucosaminyltransferase 1.The Journal of biological chemistry · 2014Article
- Dissecting the molecular basis of the role of the O-mannosylation pathway in disease: α-dystroglycan and forms of muscular dystrophy.Chembiochem : a European journal of chemical biology · 2013Review
- Novel POMGnT1 mutations cause muscle-eye-brain disease in Chinese patients.Molecular genetics and genomics : MGG · 2013Article
- Novel POMGNT1 point mutations and intragenic rearrangements associated with muscle-eye-brain disease.Journal of the neurological sciences · 2012Article
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Authors and funding
7 authors at 1 institution in 1 country.
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Abstract
Congenital muscular dystrophies have a broad spectrum of genotypes and phenotypes and there is a need for a better biochemical understanding of this group of diseases in order to aid diagnosis and treatment. Several mutations resulting in these diseases cause reduced O-mannosyl glycosylation of glycoproteins, including α-dystroglycan. The enzyme POMGnT1 (protein-O-mannose N-acetylglucosaminyltransferase 1; EC 2.4.1.-) catalyses the transfer of N-acetylglucosamine to O-linked mannose of α-dystroglycan. In the present paper we describe the biochemical characterization of 14 clinical mutants of the glycosyltransferase POMGnT1, which have been linked to muscle-eye-brain disease or similar conditions. Truncated mutant variants of the human enzyme (recombinant POMGnT1) were expressed in Escherichia coli and screened for catalytic activity. We find that three mutants show some activity towards mannosylated peptide substrates mimicking α-dystroglycan; the residues affected by these mutants are predicted by homology modelling to be on the periphery of the POMGnT1 surface. Only in part does the location of a previously described mutated residue on the periphery of the protein structure correlate with a less severe disease mutant.
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