Open AccessCatabolite inactivation of the yeast maltose transporter requires ubiquitin‐ligase npi1/rsp5 and ubiquitin‐hydrolase npi2/doa4
Author(s) -
Lucero Pilar,
Lagunas Rosario
Publication year - 1997
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1997.tb10253.x
Subject(s) - catabolite repression , ubiquitin , ubiquitin ligase , biochemistry , endocytosis , internalization , saccharomyces cerevisiae , biology , chemistry , microbiology and biotechnology , yeast , mutant , receptor , gene
The maltose transporter in Saccharomyces cerevisiae is degraded in the vacuole after internalization by endocytosis when protein synthesis is impaired and a fermentable substrate is present. The possible implication of the ubiquitin pathway in this inactivation, known as catabolite inactivation, has been investigated. Using mutants deficient in npi1/rsp5 ubiquitin‐protein ligase and npi2/doa4 ubiquitin‐protein hydrolase, we have shown that these two enzymes are required for normal endocytosis and degradation of the transporter. These facts indicate that the ubiquitin pathway is involved in catabolite inactivation of the maltose transporter. The results also revealed that both enzymes act in the internalization step of endocytosis.