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Journal of Bacteriology, May 2001, p. 3083-3088, Vol. 183, No. 10
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.10.3083-3088.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Glucose-Induced Monoubiquitination of the Saccharomyces cerevisiae Galactose Transporter Is Sufficient To Signal Its Internalization

Jaroslav Horak1 and Dieter H. Wolf2,*

Institute of Physiology, Department of Membrane Transport, Academy of Sciences of the Czech Republic,1 142 20 Prague, Czech Republic, and Institut für Biochemie der Universität Stuttgart, D-70569 Stuttgart, Germany2

Received 2 January 2001/Accepted 27 February 2001

In Saccharomyces cerevisiae, the addition of glucose to cells growing on galactose induces internalization of the galactose transporter Gal2p and its subsequent proteolysis in the vacuole. Here we report that the essential step in Gal2p down-regulation is its ubiquitination through the Ubc1p-Ubc4p-Ubc5p triad of ubiquitin-conjugating enzymes and Npi1/Rsp5p ubiquitin-protein ligase. Moreover, Gal2p appears to be stabilized in mutant cells defective in the ubiquitin-hydrolase Npi2p/Doa4p, and the mutant phenotype can be reversed by overexpression of ubiquitin. An analysis of the fate of Gal2p in cells overexpressing wild-type ubiquitin as well as its variants incompetent to form polyubiquitin chains showed that monoubiquitination of Gal2p is sufficient to signal internalization of the protein into the endocytic pathway.

* Corresponding author. Mailing address: Institut für Biochemie, Universität Stuttgart, Pfaffenwaldring 55, 70569 Stuttgart, Germany. Phone: 49-711-685-4390. Fax: 49-711-685-4392. E-mail: dieter.wolf{at}po.uni-stuttgart.de.

Journal of Bacteriology, May 2001, p. 3083-3088, Vol. 183, No. 10
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.10.3083-3088.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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