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Dystroglycan Function Requires Xylosyl- and Glucuronyltransferase Activities of LARGE

2012; American Association for the Advancement of Science; Volume: 335; Issue: 6064 Linguagem: Inglês

10.1126/science.1214115

1095-9203

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

Cell Adhesion Molecules Research

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.