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A more recent version of this article appeared on April 1, 2004
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Submitted on July 21, 2003
Revised on December 5, 2003
Accepted on December 11, 2003
1 Max Planck Institute of Molecular Cell Biology and Genetics Pfotenhauerstrasse 108, 01307 Dresden, Germany
2 Max Planck Institute of Molecular Cell Biology and Genetics Pfotenhauerstrasse 108, 01307 Dresden, Germany, , Department of Biochemistry and Biophysics, University of California, San Francisco. 513 Parnassus Avenue, San Francisco, CA 94143-0448
* Corresponding author. E-mail address: Simons{at}mpi-cbg.de.
Little is known about the mechanisms that determine localization of proteins to the plasma membrane in S. 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.
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