NCBI PubMed ID:17587671 Publication DOI:10.1271/bbb.70080 Journal NLM ID:9205717 Publisher: Japan Society for Bioscience, Biotechnology, and Agrochemistry Correspondence: m_gotoagr.kyushu-u.ac.jp Institutions: Department of Bioscience and Biotechnology, Faculty of Agriculture, Kyushu University, Japan
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.
O-glycosylation, Aspergillus, protein O-mannosyltransferase
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