Dystroglycan Glycosylation and Its Involvement in Muscular Dystrophy

被引:4
作者
Kanagawa, Motoi [1 ]
机构
[1] Kobe Univ, Grad Sch Med, Div Mol Brain Sci, Kobe, Hyogo 6500017, Japan
关键词
dystroglycan; O-mannosyl glycosylation; muscular dystrophy; fukutin; gene therapy; HUMAN LARGE GENE; ALPHA-DYSTROGLYCAN; LAMININ-BINDING; FUKUYAMA-TYPE; DEFECTIVE GLYCOSYLATION; ABNORMAL GLYCOSYLATION; GLYCOPROTEIN COMPLEX; MEMBRANE INTEGRITY; MISSENSE MUTATIONS; FUKUTIN PROTEIN;
D O I
10.4052/tigg.26.41
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Dystroglycan is a highly glycosylated peripheral membrane protein that functions as a cell surface receptor for proteins in the extracellular matrices and synapses. O-Mannosyl glycosylation is necessary for the ligand-binding activities of dystroglycan and a unique "post-phosphoryl moiety" modified via a phosphodiester linkage on the O-mannose likely forms the ligand-binding domain. Several proteins are involved in the process of this modification, the mechanism for which appears highly ordered. In various tissues, dystroglycan plays important physiological roles such as maintenance of muscle cell viability and structural development of the brain. Conversely, abnormal glycosylation causes a group of muscular dystrophy, collectively called "dystroglycanopathy," which is often associated with brain abnormalities including type II lissencephaly and mental retardation. Here, we will be reviewing the structure, modification pathway, and physiological roles of dystroglycan glycosylation as well as their involvement in human diseases.
引用
收藏
页码:41 / 57
页数:17
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