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

doi:10.1083/jcb.145.6.1177

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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 $alpha$ cells select axial sites; a/ $alpha$ cells utilize bipolar sites.Mutants specifically defective in axial budding were isolatedfrom an $alpha$ strain using pseudohyphal growth as an assay. We foundthat a and $alpha$ mutants defective in the previously identifiedPMT4 gene exhibit unipolar, rather than axial budding: mothercells choose axial bud sites, but daughter cells do not. PMT4encodes a protein mannosyl transferase (pmt) required for O-linkedglycosylation of some secretory and cell surface proteins (Immervoll,T., M. Gentzsch, and W. Tanner. 1995. Yeast. 11:1345-1351). Wedemonstrate that Axl2/Bud10p, which is required for the axialbudding pattern, is an O-linked glycoprotein and is incompletelyglycosylated, unstable, and mislocalized in cells lacking PMT4.Overexpression of AXL2 can partially restore proper bud-site selectionto pmt4 mutants. These data indicate that Axl2/Bud10p is glycosylatedby Pmt4p and that O-linked glycosylation increases Axl2/ Bud10pactivity in daughter cells, apparently by enhancing its stabilityand promoting its localization to the plasmamembrane.

Key words: O-glycosylation; PMT4; AXL2/BUD10; budding; polarity

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