Glucose-Induced Monoubiquitination of the Saccharomyces cerevisiae Galactose Transporter Is Sufficient To Signal Its Internalization
AUTOR(ES)
Horak, Jaroslav
FONTE
American Society for Microbiology
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=95208Documentos Relacionados
- Monoubiquitination Is Sufficient To Signal Internalization of the Maltose Transporter in Saccharomyces cerevisiae
- Characterization of the glucose-induced inactivation of maltose permease in Saccharomyces cerevisiae.
- Glucose-induced sequential processing of a glycosyl-phosphatidylinositol-anchored ectoprotein in Saccharomyces cerevisiae.
- Possible involvement of RAS-encoded proteins in glucose-induced inositolphospholipid turnover in Saccharomyces cerevisiae.
- Glucose-induced Crypticity Toward Succinate Metabolism in Saccharomyces lactis
