Article
Degradation of mutated bovine pancreatic trypsin inhibitor in the yeast vacuole suggests post-endoplasmic reticulum protein quality control.
The Journal of biological chemistry - 9 Apr 2004
Coughlan Christina M, Walker Jennifer L, Cochran Jared C, Wittrup K Dane, Brodsky Jeffrey L
Abstract excerpt
The rate-limiting step in protein secretion is folding, which occurs in the endoplasmic reticulum (ER) lumen, and almost all secreted proteins contain disulfide bonds that form in the ER and stabilize the native state. Secreted proteins unable to fold may aggregate or they may be subject to ER-associated protein degradation. To examine the fate of aberrant forms of a well characterized, disulfide-bonded secreted...
Topics
- Animals
- Aprotinin
- Calnexin
- Cattle
- Centrifugation, Density Gradient
- Concanavalin A
- Cycloheximide
- Cysteine Endopeptidases
- Disulfides
- Endoplasmic Reticulum
- Fluorescent Antibody Technique, Indirect
- Fungal Proteins
- Genotype