title: O-Mannosylation and human disease.
abstract: Glycosylation of proteins is arguably the most prevalent co- and post-translational modification. It is responsible for increased heterogeneity and functional diversity of proteins. Here we discuss the importance of one type of glycosylation, specifically O-mannosylation and its relationship to a number of human diseases. The most widely studied O-mannose modified protein is alpha-dystroglycan (α-DG). Recent studies have focused intensely on α-DG due to the severity of diseases associated with its improper glycosylation. O-mannosylation of α-DG is involved in cancer metastasis, arenavirus entry, and multiple forms of congenital muscular dystrophy [1, 2]. In this review, we discuss the structural and functional characteristics of O-mannose-initiated glycan structures on α-DG, enzymes involved in the O-mannosylation pathway, and the diseases that are a direct result of disruptions within this pathway.
authors.affiliation: Department of Biochemistry and Molecular Biology, Complex Carbohydrate Research Center, University of Georgia, Athens, GA, USA.
authors.forename: Christina M
authors.initials: CM
authors.lastname: Dobson
authors.forename: Samuel J
authors.initials: SJ
authors.lastname: Hempel
authors.forename: Stephanie H
authors.initials: SH
authors.lastname: Stalnaker
authors.forename: Ryan
authors.initials: R
authors.lastname: Stuart
authors.forename: Lance
authors.initials: L
authors.lastname: Wells
mesh_terms: D000818:Animals; D001117:Arenaviridae Infections / Q000235:genetics / Q000378:metabolism*; D049030:Dystroglycans / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006031:Glycosylation; D006801:Humans; D008358:Mannose / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D009136:Muscular Dystrophies / Q000235:genetics / Q000378:metabolism*; D009362:Neoplasm Metastasis; D009369:Neoplasms / Q000235:genetics / Q000378:metabolism* / Q000473:pathology
chemical_list: D049030:Dystroglycans; D008358:Mannose