RT Journal Article
SR Electronic
T1 Going LARGE
JF Science Signaling
JO Sci. Signal.
FD American Association for the Advancement of Science
SP ec16
OP ec16
DO 10.1126/scisignal.2002826
VO 5
IS 206
A1 Hurtley, Stella M.
YR 2012
UL http://stke.sciencemag.org/content/5/206/ec16.abstract
AB 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. 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. K.-i. Inamori, T. Yoshida-Moriguchi, Y. Hara, M. E. Anderson, L. Yu, K. P. Campbell, Dystroglycan function requires xylosyl- and glucuronyltransferase activities of LARGE. Science 335, 93–96 (2012). [Abstract] [Full Text]