Dystroglycan Function Requires Xylosyl- and Glucuronyltransferase Activities of LARGE

Kei-ichiro Inamori; Takako Yoshida-Moriguchi; Yuji Hara; Mary E Anderson; Liping Yu; Kevin P Campbell

doi:10.1126/science.1214115

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Dystroglycan Function Requires Xylosyl- and Glucuronyltransferase Activities of LARGE

Journal article

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Dystroglycan Function Requires Xylosyl- and Glucuronyltransferase Activities of LARGE

Kei-ichiro Inamori, Takako Yoshida-Moriguchi, Yuji Hara, Mary E Anderson, Liping Yu and Kevin P Campbell

Science (American Association for the Advancement of Science), Vol.335(6064), pp.93-96

01/06/2012

DOI: 10.1126/science.1214115

PMCID: PMC3702376

PMID: 22223806

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https://www.ncbi.nlm.nih.gov/pmc/articles/3702376View

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Abstract

Posttranslational modification of alpha-dystroglycan (α-DG) by the like-acetylglucosaminyltransferase (LARGE) is required for it to function as an extracellular matrix (ECM) receptor. Mutations in the LARGE gene have been identified in congenital muscular dystrophy patients with brain abnormalities. However, the precise function of LARGE remains unclear. Here we found that LARGE could act as a bifunctional glycosyltransferase, with both xylosyltransferase and glucuronyltransferase activities, which produced repeating units of [–3-xylose–α1,3-glucuronic acid-β1–]. This modification allowed α-DG to bind laminin-G domain–containing ECM ligands.

Details

Title: Subtitle: Dystroglycan Function Requires Xylosyl- and Glucuronyltransferase Activities of LARGE
Creators: Kei-ichiro Inamori - Howard Hughes Medical Institute, Department of Molecular Physiology and Biophysics, Department of Neurology, Department of Internal Medicine, University of Iowa Roy J. and Lucille A. Carver College of Medicine, 4283 Carver Biomedical Research Building, 285 Newton Road, Iowa City, IA 52242–1101, USA
Takako Yoshida-Moriguchi - Howard Hughes Medical Institute, Department of Molecular Physiology and Biophysics, Department of Neurology, Department of Internal Medicine, University of Iowa Roy J. and Lucille A. Carver College of Medicine, 4283 Carver Biomedical Research Building, 285 Newton Road, Iowa City, IA 52242–1101, USA
Yuji Hara - Howard Hughes Medical Institute, Department of Molecular Physiology and Biophysics, Department of Neurology, Department of Internal Medicine, University of Iowa Roy J. and Lucille A. Carver College of Medicine, 4283 Carver Biomedical Research Building, 285 Newton Road, Iowa City, IA 52242–1101, USA
Mary E Anderson - Howard Hughes Medical Institute, Department of Molecular Physiology and Biophysics, Department of Neurology, Department of Internal Medicine, University of Iowa Roy J. and Lucille A. Carver College of Medicine, 4283 Carver Biomedical Research Building, 285 Newton Road, Iowa City, IA 52242–1101, USA
Liping Yu - Medical Nuclear Magnetic Resonance Facility, University of Iowa Roy J. and Lucille A. Carver College of Medicine, B291 Carver Biomedical Research Building, 285 Newton Road, Iowa City, IA 52242–1101, USA
Kevin P Campbell - Howard Hughes Medical Institute, Department of Molecular Physiology and Biophysics, Department of Neurology, Department of Internal Medicine, University of Iowa Roy J. and Lucille A. Carver College of Medicine, 4283 Carver Biomedical Research Building, 285 Newton Road, Iowa City, IA 52242–1101, USA
Resource Type: Journal article
Publication Details: Science (American Association for the Advancement of Science), Vol.335(6064), pp.93-96
DOI: 10.1126/science.1214115
PMID: 22223806
PMCID: PMC3702376
NLM abbreviation: Science
ISSN: 0036-8075
eISSN: 1095-9203
Grant note: U54 NS053672 || NS / National Institute of Neurological Disorders and Stroke : NINDS
Language: English
Date published: 01/06/2012
Academic Unit: Neurology; Molecular Physiology and Biophysics; Iowa Neuroscience Institute; Biochemistry and Molecular Biology; Medicine Administration
Record Identifier: 9984020891202771

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