Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Sanders, S.L. et al.

Sanders, Gentzsch, Tanner, Herskowitz,

O-Glycosylation of Axl2/Bud10p by Pmt4p is required for its stability, localization, and function in daughter cells.

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 isolated from an alpha strain using pseudohyphal growth as an assay. We found that a and alpha 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.[1]

References

O-Glycosylation of Axl2/Bud10p by Pmt4p is required for its stability, localization, and function in daughter cells. Sanders, S.L., Gentzsch, M., Tanner, W., Herskowitz, I. J. Cell Biol. (1999) [Pubmed]

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