Proteasome-dependent endoplasmic reticulum-associated protein degradation: an unconventional route to a familiar fate.
Proc Natl Acad Sci U S A
; 93(24): 13797-801, 1996 Nov 26.
Article
en En
| MEDLINE
| ID: mdl-8943015
ABSTRACT
Until recently, the degradation of aberrant and unassembled proteins retained in the endoplasmic reticulum (ER) was thought to involve unidentified ER-localized proteases. We now show that the ER-associated degradation (ERAD) of two mutant proteins that accumulate in the ER lumen is inhibited in a proteasome-defective yeast strain and when cytosol from this mutant is used in an in vitro assay. In addition, ERAD is limited in vitro in the presence of the proteasome inhibitors, 3,4-dichloroisocoumarin and lactacystin. Furthermore, we find that an ERAD substrate is exported from ER-derived microsomes, and the accumulation of exported substrate is 2-fold greater when proteasome mutant cytosol is used in place of wild-type cytosol. We conclude that lumenal ERAD substrates are exported from the yeast ER to the cytoplasm for degradation by the proteasome complex.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Saccharomyces cerevisiae
/
Proteínas Fúngicas
/
Cisteína Endopeptidasas
/
Retículo Endoplásmico
/
Complejos Multienzimáticos
Tipo de estudio:
Risk_factors_studies
Idioma:
En
Revista:
Proc Natl Acad Sci U S A
Año:
1996
Tipo del documento:
Article
País de afiliación:
Estados Unidos