Cellular and Molecular Life Sciences

, Volume 70, Issue 16, pp 2849–2857

O-Mannosylation and human disease

  • Christina M. Dobson
  • Samuel J. Hempel
  • Stephanie H. Stalnaker
  • Ryan Stuart
  • Lance Wells
Review

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.

Keywords

Alpha-dystroglycan Arenavirus Cancer LARGE ISPD Metastasis Congenital muscular dystrophy Dystroglycanopathy 

Copyright information

© Springer Basel 2012

Authors and Affiliations

  • Christina M. Dobson
    • 1
  • Samuel J. Hempel
    • 1
  • Stephanie H. Stalnaker
    • 1
  • Ryan Stuart
    • 1
  • Lance Wells
    • 1
  1. 1.Department of Biochemistry and Molecular Biology, Complex Carbohydrate Research CenterUniversity of GeorgiaAthensUSA

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