| Literature DB >> 22223806 |
Kei-ichiro Inamori1, Takako Yoshida-Moriguchi, Yuji Hara, Mary E Anderson, Liping Yu, Kevin P Campbell.
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.Entities:
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Year: 2012 PMID: 22223806 PMCID: PMC3702376 DOI: 10.1126/science.1214115
Source DB: PubMed Journal: Science ISSN: 0036-8075 Impact factor: 47.728