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Vol. 15, Issue 4, 1533-1543, April 2004

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O-Glycosylation as a Sorting Determinant for Cell Surface Delivery in Yeast

Tomasz J. Proszynski, Kai Simons ^*, and Michel Bagnat 

Max Planck Institute for Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01307 Dresden, Germany

Submitted July 21, 2003; Revised December 5, 2003; Accepted December 11, 2003
Monitoring Editor: Chris Kaiser

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.

Article published online ahead of print. Mol. Biol. Cell 10.1091/mbc.E03–07–0511. Article and publication date are available at www.molbiolcell.org/cgi/doi/10.1091/mbc.E03–07–0511.

Present address: Department of Biochemistry and Biophysics, 513 Parnassus Ave., University of California, San Francisco, San Francisco, CA 94143-0448.

^* Corresponding author. E-mail address: simons{at}mpi-cbg.de.

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