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Proteasome-dependent endoplasmic reticulum-associated protein degradation: an unconventional route to a familiar fate
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Proteasome-dependent endoplasmic reticulum-associated protein degradation: an unconventional route to a familiar fate
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Journal Article
Proteasome-dependent endoplasmic reticulum-associated protein degradation: an unconventional route to a familiar fate
1996
Overview
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
Publisher
National Academy of Sciences of the United States of America,The National Academy of Sciences of the USA,National Academy of Sciences
Subject
/ Acetylcysteine - analogs & derivatives
/ Acetylcysteine - pharmacology
/ Adenosine Triphosphate - metabolism
/ Cysteine Endopeptidases - genetics
/ Cysteine Endopeptidases - metabolism
/ Cysteine Proteinase Inhibitors
/ Cysteine Proteinase Inhibitors - pharmacology
/ cytology
/ Cytosol
/ Endoplasmic Reticulum - drug effects
/ Endoplasmic Reticulum - metabolism
/ ENZIMAS
/ ENZYME
/ Enzymes
/ Fungal Proteins - metabolism
/ genetics
/ Kinetics
/ Multienzyme Complexes - genetics
/ Multienzyme Complexes - metabolism
/ MUTANT
/ MUTANTES
/ mutants
/ Mutation
/ Plasmids
/ Proteasome Endopeptidase Complex
/ PROTEINE
/ Proteins
/ Saccharomyces cerevisiae - cytology
/ Saccharomyces cerevisiae - genetics
/ Saccharomyces cerevisiae - physiology
/ Yeast
/ Yeasts
