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MBC in Press, published online ahead of print July 11, 2002
Mol. Biol. Cell 10.1091/mbc.E02-04-0186

A more recent version of this article appeared on August 1, 2002
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Submitted on April 5, 2002
Revised on May 21, 2002
Accepted on May 31, 2002

Multiple functions of sterols in yeast endocytosis

Antje Heese-Peck1, Harald Pichler2, Bettina Zanolari2, Reika Watanabe2, Günther Daum3, and Howard Riezman2*

1 Biozentrum of the University of Basel, CH-4056 Basel, Switzerland (present address: Sainsbury Laboratory, John Innes Centre, Colney Lane, Norwich NR4 7UH, England)
2 Biozentrum of the University of Basel, CH-4056 Basel, Switzerland
3 Institut für Biochemie, Technische Universität, A-8010 Graz, Austria

* Corresponding author. E-mail address: Howard.Riezman{at}unibas.ch.

Sterols are essential factors for endocytosis in animals and yeast. To investigate the sterol structural requirements for yeast endocytosis, we created a variety of erg{Delta} mutants, each accumulating a distinct set of sterols different from ergosterol. Mutant erg2{Delta}erg6{Delta} and erg3{Delta}erg6{Delta} cells exhibit a strong internalization defect of the {alpha}-factor receptor (Ste2p). Specific sterol structures are necessary for pheromone-dependent receptor hyperphosphorylation, a prerequisite for internalization. The lack of phosphorylation is not due to a defect in Ste2p localization or in ligand-receptor interaction. Contrary to most known endocytic factors, sterols appear to function in internalization independently of actin. Furthermore, sterol structures are required at a post-internalization step of endocytosis. erg{Delta} cells were able to take up the membrane marker FM4-64, but exhibited defects in FM4-64 movement through endosomal compartments to the vacuole. Therefore, there are at least two roles for sterols in endocytosis. Based on sterol analysis, the sterol structural requirements for these two processes were different suggesting that sterols may have distinct functions at different places in the endocytic pathway. Interestingly, sterol structures unable to support endocytosis allowed transport of the GPI-anchored protein, Gas1p, from the ER to Golgi compartment.




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