Protein O-glycosylation in fungi: diverse structures and multiple functions.
Protein glycosylation is essential for eukaryotic cells from yeasts to humans. When compared to N-glycosylation, O-glycosylation is variable in sugar components and the mode of linkages connecting the sugars. In fungi, secretory proteins are commonly mannosylated by protein O-mannosyltransferase (PMT) in the endoplasmic reticulum, and subsequently glycosylated by several glycosyltransferases in the Golgi apparatus to form glycoproteins with diverse O-glycan structures. Protein O-glycosylation has roles in modulating the function of secretory proteins by enhancing the stability and solubility of the proteins, by affording protection from protease degradation, and by acting as a sorting determinant in yeasts. In filamentous fungi, protein O-glycosylation contributes to proper maintenance of fungal morphology, hyphal development, and differentiation. This review describes recent studies of the structure and function of protein O-glycosylation in industrially and medically important fungi.
Goto
Masatoshi
M
Department of Bioscience and Biotechnology, Faculty of Agriculture, Kyushu University, Japan. m_goto@agr.kyushu-u.ac.jp
D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D005656:Fungal Proteins / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology; D006031:Glycosylation; D010100:Oxygen; D011499:Protein Processing, Post-Translational / Q000502:physiology*
D005656:Fungal Proteins; D010100:Oxygen