Abstract:
:Little is known about the mechanisms that determine localization of proteins to the plasma membrane in Saccharomyces cerevisiae. The length of the transmembrane domains and association of proteins with lipid rafts have been proposed to play a role in sorting to the cell surface. Here, we report that Fus1p, an O-glycosylated integral membrane protein involved in cell fusion during yeast mating, requires O-glycosylation for cell surface delivery. In cells lacking PMT4, encoding a mannosyltransferase involved in the initial step of O-glycosylation, Fus1p was not glycosylated and accumulated in late Golgi structures. A chimeric protein lacking O-glycosylation motif was missorted to the vacuole and accumulated in late Golgi in wild-type cells. Exocytosis of this protein could be restored by addition of a 33-amino acid portion of an O-glycosylated sequence from Fus1p. Our data suggest that O-glycosylation functions as a sorting determinant for cell surface delivery of Fus1p.
journal_name
Mol Biol Celljournal_title
Molecular biology of the cellauthors
Proszynski TJ,Simons K,Bagnat Mdoi
10.1091/mbc.e03-07-0511keywords:
subject
Has Abstractpub_date
2004-04-01 00:00:00pages
1533-43issue
4eissn
1059-1524issn
1939-4586pii
E03-07-0511journal_volume
15pub_type
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