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Ribitol-phosphate—a newly identified posttranslational glycosylation unit in mammals: structure, modification enzymes and relationship to human diseases
- Source :
- The Journal of Biochemistry. 163:359-369
- Publication Year :
- 2018
- Publisher :
- Oxford University Press (OUP), 2018.
-
Abstract
- Glycosylation is a crucial posttranslational modification that is involved in numerous biological events. Therefore, abnormal glycosylation can impair the functions of glycoproteins or glycolipids and is occasionally associated with cell dysfunction and human diseases. For example, aberrant glycosylation of dystroglycan (DG), a cellular receptor for matrix and synaptic proteins, is associated with muscular dystrophy and lissencephaly. DG sugar chains are required for high-affinity binding to ligand proteins, and thus disruption of DG-ligand linkages underlies disease conditions. Although their biological significance is well recognized, the sugar-chain structure of DG and its modification enzymes have long remained incompletely elucidated. However, recent seminal studies have finally revealed a highly regulated mechanism for DG glycosylation and have discovered a posttranslational unit, ribitol-phosphate, that was not previously known to be used in mammals. This review article introduces the structure, modification enzymes and functions of the sugar chains of DG, and then discusses their relationship to human diseases and therapeutic strategies .
- Subjects :
- 0301 basic medicine
Glycosylation
Protein Conformation
Cell
Biochemistry
Muscular Dystrophies
Abnormal glycosylation
03 medical and health sciences
chemistry.chemical_compound
Protein structure
Dystroglycan
medicine
Animals
Humans
Muscular dystrophy
Dystroglycans
Molecular Biology
chemistry.chemical_classification
Pentosephosphates
biology
Glycosyltransferases
General Medicine
medicine.disease
carbohydrates (lipids)
030104 developmental biology
Enzyme
medicine.anatomical_structure
chemistry
biology.protein
Glycoprotein
Subjects
Details
- ISSN :
- 17562651 and 0021924X
- Volume :
- 163
- Database :
- OpenAIRE
- Journal :
- The Journal of Biochemistry
- Accession number :
- edsair.doi.dedup.....163ee9e8e0ce9b394b4d16142262bcfb