Dystroglycan Function Requires Xylosyl- and Glucuronyltransferase Activities of LARGE-Reference-Cited by-同舟云学术

Dystroglycan Function Requires Xylosyl- and Glucuronyltransferase Activities of LARGE

Published:2012-01-06 Issue:6064 Volume:335 Page:93-96
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Inamori Kei-ichiro¹,Yoshida-Moriguchi Takako¹,Hara Yuji¹,Anderson Mary E.¹,Yu Liping²,Campbell Kevin P.¹

Affiliation:

1. 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.

2. 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.

Abstract

Going LARGE Dystroglycan (DG) is a highly glycosylated extracellular matrix (ECM) receptor involved in a variety of physiological processes, including maintenance of skeletal muscle membrane integrity and the structure and function of the central nervous system. The like-acetylglucosaminyltransferase (LARGE) is responsible for posttranslational modifications of alpha-dystroglycan (α-DG) required for its function. Now, Inamori et al. (p. 93 ) demonstrate that LARGE is a bifunctional glycosyltransferase able to transfer xylose and glucuronic acid. These modifications allow α-DG to bind the laminin-G domain–containing ECM ligands: laminin, agrin, and neurexin.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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