'ER degradation' of a mutant yeast plasma membrane protein by the ubiquitin-proteasome pathway.
FASEB J
; 12(3): 315-23, 1998 Mar.
Article
en En
| MEDLINE
| ID: mdl-9506475
The yeast plasma membrane, uracil permease, undergoes ubiquitin-dependent endocytosis and subsequent degradation in the vacuole via a process that does not involve the proteasome. Cell-surface ubiquitination of this protein is mediated by the ubiquitin-protein ligase Npi1p/Rsp5p and involves Lys63-linked ubiquitin chains. This report describes the intracellular fate of a mutant form of uracil permease carrying a three amino acid insertion in a cytoplasmic loop. Most of this protein is not deployed beyond the ER, and is degraded by the 26S proteasome. Mutant permease degradation is almost unaffected in cells with impaired Npi1p/Rsp5p, but is dependent on the Ubc6p and Ubc7p ubiquitin-conjugating enzymes, suggesting that proteolysis of the protein requires its prior ubiquitination. Overproduction of a derivative of ubiquitin with a modified Lys48 strongly impairs mutant permease degradation. This suggests that, like other proteasome substrates, mutant permease might be polyubiquitinated with Lys48-linked ubiquitin chains. These findings provide an example of a yeast plasma membrane protein that is routed to the 'ER degradation' pathway, and highlight the versatility of the ubiquitin system.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas de Transporte de Membrana
/
Saccharomyces cerevisiae
/
Cisteína Endopeptidasas
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Ubiquitinas
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Proteínas de Saccharomyces cerevisiae
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Proteínas de Transporte de Nucleótidos
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Proteínas de la Membrana
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Complejos Multienzimáticos
/
Mutación
Idioma:
En
Revista:
FASEB J
Asunto de la revista:
BIOLOGIA
/
FISIOLOGIA
Año:
1998
Tipo del documento:
Article
País de afiliación:
Francia
Pais de publicación:
Estados Unidos