Synthesis of sphingolipids with very long chain fatty acids but not Ergosterol is required for routing of newly synthesized plasma membrane ATPase to the cell surface of yeast
- Gaigg, Barbara Division of Biochemistry, Department of Medicine, University of Fribourg, Switzerland
- Timischl, Birgit Division of Biochemistry, Department of Medicine, University of Fribourg, Switzerland
- Corbino, Linda Division of Biochemistry, Department of Medicine, University of Fribourg, Switzerland
- Schneiter, Roger Division of Biochemistry, Department of Medicine, University of Fribourg, Switzerland
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10.06.2005
Published in:
- Journal of Biological Chemistry. - 2005, vol. 280, no. 3, p. 22515-22522
English
The proton pumping H⁺-ATPase, Pma1p, is an abundant and very long-lived polytopic protein of the Saccharomyces cerevisiae plasma membrane. Pma1p constitutes a major cargo of the secretory pathway and thus serves as an excellent model to study plasma membrane biogenesis. We have previously shown that newly synthesized Pma1p is mistargeted to the vacuole in an elo3δ mutant that affects the synthesis of the ceramide-bound C26 very long chain fatty acid (Eisenkolb, M., Zenzmaier, C., Leitner, E., and Schneiter, R. (2002) Mol. Biol. Cell 13, 4414–4428) and now describe a more detailed analysis of the role of lipids in Pma1p biogenesis. Remarkably, a block at various steps of sterol biosynthesis, a complete block in sterol synthesis, or the substitution of internally synthesized ergosterol by externally supplied ergosterol or even by cholesterol does not affect Pma1p biogenesis or its association with detergent-resistant membrane domains (lipid "rafts"). However, a block in sphingolipid synthesis or any perturbation in the synthesis of the ceramide-bound C26 very long chain fatty acid results in mistargeting of newly synthesized Pma1p to the vacuole. Mistargeting correlates with a lack of newly synthesized Pma1p to acquire detergent resistance, suggesting that sphingolipids with very long acyl chains affect sorting of Pma1p to the cell surface.
- Faculty
- Faculté des sciences et de médecine
- Department
- Département de Biologie
- Language
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- English
- Classification
- Biological sciences
- License
- License undefined
- Identifiers
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- RERO DOC 5146
- DOI 10.1074/jbc.M413472200
- Persistent URL
- https://folia.unifr.ch/unifr/documents/299947
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