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Review
. 2013 Mar 8;288(10):6930-5.
doi: 10.1074/jbc.R112.438978. Epub 2013 Jan 17.

The o-mannosylation pathway: glycosyltransferases and proteins implicated in congenital muscular dystrophy

Lance Wells  1
Affiliations
Review

The o-mannosylation pathway: glycosyltransferases and proteins implicated in congenital muscular dystrophy

Lance Wells. J Biol Chem. .

Abstract

Several forms of congenital muscular dystrophy, referred to as dystroglycanopathies, result from defects in the protein O-mannosylation biosynthetic pathway. In this minireview, I discuss 12 proteins involved in the pathway and how they play a role in the building of glycan structures (most notably on the protein α-dystroglycan) that allow for binding to multiple proteins of the extracellular matrix.

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Figures

FIGURE 1.
FIGURE 1.
O-Mannose structures. O-Man-initiated glycans can be elaborated into linear or branched structures. A key structure for binding to extracellular matrix proteins is not fully resolved but contains a phosphodiester linkage, and a component of the X moiety is likely to be the LARGE-catalyzed repeating disaccharide. Green circles, Man; blue squares, GlcNAc; yellow square, GalNAc; yellow circles, Gal; pink diamonds, Neu5Ac; red triangles, Fuc; orange star, Xyl; blue/white diamond, GlcUA. GlcNAc residues on the O-Man added in the 2-position are drawn up to the left, in the 4-position straight up, and in the 6-position up to the right. Asymmetric branched structures are drawn in only one possible configuration, although isomeric structures are likely to exist.
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References

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