Xylosyl- and glucuronyltransferase LARGE2

Definition:

Bifunctional glycosyltransferase with both alpha-1,3-xylosyltransferase and beta-1,3-glucuronyltransferase activities involved in the maturation of alpha-dystroglycan (DAG1) by glycosylation leading to DAG1 binding to laminin G-like domain-containing extracellular proteins with high affinity and in a phosphorylated-O-mannosyl trisaccharide dependent manner. Elongates the glucuronyl-beta-1,4-xylose-beta disaccharide primer structure by adding repeating units [-3-Xylose-alpha-1,3-GlcA-beta-1-] to produce a heteropolysaccharide (By similarity). Supports the maturation of DAG1 more effectively than LARGE1. In addition, can modify both heparan sulfate (HS)- and chondroitin/dermatan sulfate (CS/DS)-proteoglycans (PGs), namely GPC4, with a glycosaminoglycan (GAG)-like polysaccharide composed of xylose and glucuronic acid to confer laminin binding (By similarity).

References:

[1]. Katsuya Fujimura, et al. LARGE2 facilitates the maturation of alpha-dystroglycan more effectively than LARGE. Biochem Biophys Res Commun. 2005 Apr 15;329(3):1162-71. [Content Brief]

[2]. Martin Brockington, et al. Localization and functional analysis of the LARGE family of glycosyltransferases: significance for muscular dystrophy. Hum Mol Genet. 2005 Mar 1;14(5):657-65. [Content Brief]

[3]. Kei-ichiro Inamori, et al. Endogenous glucuronyltransferase activity of LARGE or LARGE2 required for functional modification of α-dystroglycan in cells and tissues. J Biol Chem. 2014 Oct 10;289(41):28138-48. [Content Brief]

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