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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 (?-DG). Recent studies have focused intensely on ?-DG due to the severity of diseases associated with its improper glycosylation. O-mannosylation of ?-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 ?-DG, enzymes involved in the O-mannosylation pathway, and the diseases that are a direct result of disruptions within this pathway.

SUBMITTER: Dobson CM

PROVIDER: S-EPMC3984002 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature

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O-Mannosylation and human disease.

Dobson Christina M CM Hempel Samuel J SJ Stalnaker Stephanie H SH Stuart Ryan R Wells Lance L

Cellular and molecular life sciences : CMLS 20121101 16

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 i ...[more]

PMID: 23115008

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