A PEST-like sequence mediates phosphorylation and efficient ubiquitination of yeast uracil permease.

ABSTRACT: Uptake of uracil by the yeast Saccharomyces cerevisiae is mediated by a specific permease encoded by the FUR4 gene. Uracil permease located at the cell surface is subject to two covalent modifications: phosphorylation and ubiquitination. The ubiquitination step is necessary prior to permease endocytosis and subsequent vacuolar degradation. Here, we demonstrate that a PEST-like sequence located within the cytoplasmic N terminus of the protein is essential for uracil permease turnover. Internalization of the transporter was reduced when some of the serines within the region were converted to alanines and severely impaired when all five serines within the region were mutated or when this region was absent. The phosphorylation and degree of ubiquitination of variant permeases were inversely co

SUBMITTER: Marchal C 

PROVIDER: S-EPMC121498 | biostudies-literature | 1998 Jan

REPOSITORIES: biostudies-literature