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Eukaryotic Cell, October 2004, p. 1164-1168, Vol. 3, No. 5
1535-9778/04/$08.00+0     DOI: 10.1128/EC.3.5.1164-1168.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Pmt-Mediated O Mannosylation Stabilizes an Essential Component of the Secretory Apparatus, Sec20p, in Candida albicans

Yvonne Weber, Stephan K.-H. Prill, and Joachim F. Ernst*

Institut für Mikrobiologie, Heinrich-Heine-Universität, Düsseldorf, Germany

Received 14 May 2004/ Accepted 30 June 2004

Sec20p is an essential endoplasmic reticulum (ER) membrane protein in yeasts, functioning as a tSNARE component in retrograde vesicle traffic. We show that Sec20p in the human fungal pathogen Candida albicans is extensively O mannosylated by protein mannosyltransferases (Pmt proteins). Surprisingly, Sec20p occurs at wild-type levels in a pmt6 mutant but at very low levels in pmt1 and pmt4 mutants and also after replacement of specific Ser/Thr residues in the lumenal domain of Sec20p. Pulse-chase experiments revealed rapid degradation of unmodified Sec20p (38.6 kDa) following its biosynthesis, while the stable O-glycosylated form (50 kDa) was not formed in a pmt1 mutant. These results suggest a novel function of O mannosylation in eukaryotes, in that modification by specific Pmt proteins will prevent degradation of ER-resident membrane proteins via ER-associated degradation or a proteasome-independent pathway.

* Corresponding author. Mailing address: Institut für Mikrobiologie Heinrich-Heine-Universität Düsseldorf, Universitätsstr. 1/Geb. 26.12, D-40225 Düsseldorf, Germany. Phone and fax: 49 (211) 811-5176. E-mail: joachim.ernst{at}uni-duesseldorf.de.

Eukaryotic Cell, October 2004, p. 1164-1168, Vol. 3, No. 5
1535-9778/04/$08.00+0     DOI: 10.1128/EC.3.5.1164-1168.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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