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- W1975456619 endingPage "307" @default.
- W1975456619 startingPage "297" @default.
- W1975456619 abstract "Protein O-mannosylation, originally observed in fungi, starts at the endoplasmic reticulum with the transfer of mannose from dolichyl activated mannose to seryl or threonyl residues of secretory proteins. This reaction is catalyzed by a family of protein O-mannosyltransferases (PMTs), which were first characterized in Saccharomyces cerevisiae. The identification of this evolutionarily conserved PMT gene family has led to the finding that protein O-mannosylation plays an essential role in a number of physiologically important processes. Focusing on the PMT gene family, we discuss here the main aspects of the biogenesis of O-linked carbohydrate chains in S. cerevisiae, Candida albicans, and other fungi. We summarize recent work utilizing pmt mutants that demonstrates the impact of protein O-mannosylation on protein secretion, on maintenance of cell wall integrity, and on budding. Further, the occurrence of PMT orthologs in higher eukaryotes such as Arabidopsis, Drosophila and mammals is reported and discussed." @default.
- W1975456619 created "2016-06-24" @default.
- W1975456619 creator A5018568459 @default.
- W1975456619 creator A5047498334 @default.
- W1975456619 creator A5052559958 @default.
- W1975456619 date "1999-01-01" @default.
- W1975456619 modified "2023-10-10" @default.
- W1975456619 title "Protein O-mannosylation" @default.
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