ArticleGlycobiology2009
Mutational and functional analysis of Large in a novel CHO glycosylation mutant.
Article in Glycobiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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Who cites it
27 citing papers in PubMed, 36 citations in OpenAlex.
- Cell surface glycan engineering reveals that matriglycan alone can recapitulate dystroglycan binding and function.Nature communications · 2022Article
- Defective mucin-type glycosylation on α-dystroglycan in COG-deficient cells increases its susceptibility to bacterial proteases.The Journal of biological chemistry · 2018Article
- Recent advancements in understanding mammalian O-mannosylation.Glycobiology · 2017Review
- Article
- Global serum glycoform profiling for the investigation of dystroglycanopathies & Congenital Disorders of Glycosylation.Molecular genetics and metabolism reports · 2016Article
- Rapid assays for lectin toxicity and binding changes that reflect altered glycosylation in mammalian cells.Current protocols in chemical biology · 2014Article
- Mammalian O-mannosylation pathway: glycan structures, enzymes, and protein substrates.Biochemistry · 2014Review
- Antibodies that detect O-linked β-D-N-acetylglucosamine on the extracellular domain of cell surface glycoproteins.The Journal of biological chemistry · 2014Article
- The transgenic expression of LARGE exacerbates the muscle phenotype of dystroglycanopathy mice.Human molecular genetics · 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
- O-Mannosylation and human disease.Cellular and molecular life sciences : CMLS · 2013Review
- Xylosyl- and glucuronyltransferase functions of LARGE in α-dystroglycan modification are conserved in LARGE2.Glycobiology · 2013Article
- Adeno-associated viral-mediated LARGE gene therapy rescues the muscular dystrophic phenotype in mouse models of dystroglycanopathy.Human gene therapy · 2013Article
- High throughput screening for compounds that alter muscle cell glycosylation identifies new role for N-glycans in regulating sarcolemmal protein abundance and laminin binding.The Journal of biological chemistry · 2012Article
- Glycosylation of α-dystroglycan: O-mannosylation influences the subsequent addition of GalNAc by UDP-GalNAc polypeptide N-acetylgalactosaminyltransferases.The Journal of biological chemistry · 2012Article
- Identification of mono- and disulfated N-acetyl-lactosaminyl Oligosaccharide structures as epitopes specifically recognized by humanized monoclonal antibody HMOCC-1 raised against ovarian cancer.The Journal of biological chemistry · 2012Article
- Differential glycosylation of α-dystroglycan and proteins other than α-dystroglycan by like-glycosyltransferase.Glycobiology · 2012Article
- Second international workshop for glycosylation defects in muscular dystrophies, 11-12 November, 2010, Charlotte, USA.Brain pathology (Zurich, Switzerland) · 2011Article
- Mammalian O-mannosylation: unsolved questions of structure/function.Current opinion in structural biology · 2011Review
- Golgi glycosylation and human inherited diseases.Cold Spring Harbor perspectives in biology · 2011Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Inactivating mutations of Large reduce the functional glycosylation of alpha-dystroglycan (alpha-DG) and lead to muscular dystrophy in mouse and humans. The N-terminal domain of Large is most similar to UDP-glucose glucosyltransferases (UGGT), and the C-terminal domain is related to the human i blood group transferase beta1,3GlcNAcT-1. The amino acids at conserved motifs DQD+1 and DQD+3 in the UGGT domain are necessary for mammalian UGGT activity. When the corresponding residues were mutated to Ala in mouse Large, alpha-DG was not functionally glycosylated. A similar result was obtained when a DXD motif in the beta1,3GlcNAcT-1 domain was mutated to AIA. Therefore, the first putative glycosyltransferase domain of Large has properties of a UGGT and the second of a typical glycosyltransferase. Co-transfection of Large mutants affected in the different glycosyltransferase domains did not lead to complementation. While Large mutants were more localized to the endoplasmic reticulum than wild-type Large or revertants, all mutants were in the Golgi, and only very low levels of Golgi-localized Large were necessary to generate functional alpha-DG. When Large was overexpressed in ldlD.Lec1 mutant Chinese hamster ovary (CHO) cells which synthesize few, if any, mucin O-GalNAc glycans and no complex N-glycans, functional alpha-DG was produced, presumably by modifying O-mannose glycans. To investigate mucin O-GalNAc glycans as substrates of Large, a new CHO mutant Lec15.Lec1 that lacked O-mannose and complex N-glycans was isolated and characterized. Following transfection with Large, Lec15.Lec1 cells also generated functionally glycosylated alpha-DG. Thus, Large may act on the O-mannose, complex N-glycans and mucin O-GalNAc glycans of alpha-DG.
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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.