Related Experiment Video
Updated: Aug 11, 2025

DNA Electroporation, Isolation and Imaging of Myofibers
Published on: December 23, 2015
Inhibitory machinery for the functional dystroglycan glycosylation
Yuji Kondo1,2, Tetsuya Okajima1,2
1Department of Molecular Biochemistry, Nagoya University Graduate School of Medicine, Nagoya 466-8550, Japan.
Abstract:
Dystroglycan (DG), a muscular transmembrane protein, plays a critical role in transducing extracellular matrix-derived signals to the cytoskeleton and provides physical strength to skeletal muscle cell membranes. The extracellular domain of DG, α-DG, displays unique glycosylation patterns. Fully functional glycosylation is required for this domain to interact with components of extracellular matrices, including laminin. One of the unique sugar compositions found in such functional glycans on DG is two ribitol phosphates that are transferred by the sequential actions of fukutin (FKTN) and fukutin-related protein (FKRP), which use CDP-ribitol as a donor substrate. These are then further primed for matriglycan biosynthesis. A recent in vitro study reported that glycerol phosphate could be similarly added to α-DG by FKTN and FKRP if they used CDP-glycerol (CDP-Gro) as a donor substrate. However, the physiological relevance of these findings remains elusive. Imae et al. addressed the knowledge gap regarding whether CDP-Gro is present in mammals and how CDP-Gro is synthesized and functions in mammals.
Related Concept Videos
Oligosaccharide Assembly
Multiple sugar molecules that may or may...
Proteoglycans
Lysosomal Hydrolases
Protein Folding Quality Check in the RER
Export of Misfolded Proteins out of the ER
Protein Glycosylation
Glycosylation occurs in...

