J. Cell Biol., Volume 145, Number 6, June 14, 1999 1177-1188

O-Glycosylation of Axl2/Bud10p by Pmt4p Is Required for Its Stability, Localization, and Function in Daughter Cells

Sylvia L. Sanders,^* Martina Gentzsch, Widmar Tanner, and Ira Herskowitz^*

^* Department of Biochemistry and Biophysics, University of California, San Francisco, California 94143-0448; and  Lehrstuhl für Zellbiologie und Pflanzenphysiologie, Universität Regensburg, D-93053 Regensburg, Germany

Cells of the yeast Saccharomyces cerevisiae choose bud sites in a manner that is dependent upon cell type: a and  cells select axial sites; a/ cells utilize bipolar sites. Mutants specifically defective in axial budding were isolated from an  strain using pseudohyphal growth as an assay. We found that a and  mutants defective in the previously identified PMT4 gene exhibit unipolar, rather than axial budding: mother cells choose axial bud sites, but daughter cells do not. PMT4 encodes a protein mannosyl transferase (pmt) required for O-linked glycosylation of some secretory and cell surface proteins (Immervoll, T., M. Gentzsch, and W. Tanner. 1995. Yeast. 11:1345-1351). We demonstrate that Axl2/Bud10p, which is required for the axial budding pattern, is an O-linked glycoprotein and is incompletely glycosylated, unstable, and mislocalized in cells lacking PMT4. Overexpression of AXL2 can partially restore proper bud-site selection to pmt4 mutants. These data indicate that Axl2/Bud10p is glycosylated by Pmt4p and that O-linked glycosylation increases Axl2/ Bud10p activity in daughter cells, apparently by enhancing its stability and promoting its localization to the plasma membrane.

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