O-mannosyl glycans: from yeast to novel associations with human disease

Curr Opin Struct Biol. 2003 Oct;13(5):621-30. doi: 10.1016/j.sbi.2003.09.003.

Abstract

In yeasts and other fungi, O-mannosyl glycans constitute a major protein modification that is essential for cell viability. For several decades, protein O-mannosylation was considered a yeast-specific modification. Thus, it was especially interesting when it became evident that O-mannosyl glycans in mammals are not as rare as previously thought. O-mannosyl glycans are abundant in the mammalian brain and are also an abundant modification of alpha-dystroglycan, a component of the dystrophin-glycoprotein complex. Recently, mutations in genes that are or might be involved in the glycosylation of alpha-dystroglycan have been identified. Their association with neuromuscular diseases has focused the attention of different research areas on protein O-mannosylation.

Publication types

  • Comparative Study
  • Review

MeSH terms

  • Animals
  • Glycoproteins / chemistry*
  • Glycoproteins / metabolism*
  • Humans
  • Mammals
  • Mannose / chemistry
  • Mannose / metabolism
  • Mannosyltransferases / chemistry
  • Mannosyltransferases / metabolism
  • Molecular Conformation
  • Molecular Structure
  • Muscular Dystrophies / metabolism*
  • Polysaccharides / chemistry*
  • Polysaccharides / metabolism*
  • Saccharomyces cerevisiae / chemistry
  • Saccharomyces cerevisiae / metabolism
  • Species Specificity
  • Structure-Activity Relationship
  • Yeasts / chemistry*
  • Yeasts / metabolism*

Substances

  • Glycoproteins
  • Polysaccharides
  • Mannosyltransferases
  • protein O-mannosyltransferase
  • Mannose