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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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