Nitrogen coordinated import and export of arginine across the yeast vacuolar membrane.
PLoS Genet
; 16(8): e1008966, 2020 08.
Article
en En
| MEDLINE
| ID: mdl-32776922
ABSTRACT
The vacuole of the yeast Saccharomyces cerevisiae plays an important role in nutrient storage. Arginine, in particular, accumulates in the vacuole of nitrogen-replete cells and is mobilized to the cytosol under nitrogen starvation. The arginine import and export systems involved remain poorly characterized, however. Furthermore, how their activity is coordinated by nitrogen remains unknown. Here we characterize Vsb1 as a novel vacuolar membrane protein of the APC (amino acid-polyamine-organocation) transporter superfamily which, in nitrogen-replete cells, is essential to active uptake and storage of arginine into the vacuole. A shift to nitrogen starvation causes apparent inhibition of Vsb1-dependent activity and mobilization of stored vacuolar arginine to the cytosol. We further show that this arginine export involves Ypq2, a vacuolar protein homologous to the human lysosomal cationic amino acid exporter PQLC2 and whose activity is detected only in nitrogen-starved cells. Our study unravels the main arginine import and export systems of the yeast vacuole and suggests that they are inversely regulated by nitrogen.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Arginina
/
Saccharomyces cerevisiae
/
Proteínas de Saccharomyces cerevisiae
/
Nitrógeno
Límite:
Humans
Idioma:
En
Año:
2020
Tipo del documento:
Article