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Vol. 12, Issue 4, 1047-1059, April 2001
Institut für Mikrobiologie, Heinrich-Heine-Universität
Düsseldorf, D-40225 Düsseldorf, Germany
Previous experiments suggested that trafficking of the
a-factor transporter Ste6 of Saccharomyces
cerevisiae to the yeast vacuole is regulated by ubiquitination. To
define the ubiquitination-dependent step in the trafficking pathway, we
examined the intracellular localization of Ste6 in the
ubiquitination-deficient doa4 mutant by immunofluorescence
experiments, with a Ste6-green fluorescent protein fusion
protein and by sucrose density gradient fractionation. We found that
Ste6 accumulated at the vacuolar membrane in the doa4 mutant
and not at the cell surface. Experiments with a doa4 pep4
double mutant showed that Ste6 uptake into the lumen of the vacuole is
inhibited in the doa4 mutant. The uptake defect could be
suppressed by expression of additional ubiquitin, indicating that it is
primarily the result of a lowered ubiquitin level (and thus of reduced
ubiquitination) and not the result of a deubiquitination defect. Based
on our findings, we propose that ubiquitination of Ste6 or of a
trafficking factor is required for Ste6 sorting into the multivesicular
bodies pathway. In addition, we obtained evidence suggesting that Ste6
recycles between an internal compartment and the plasma membrane.
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