N-Glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast
The endoplasmic reticulum (ER) of eukaryotic cells contains a quality control system, that is required for the proteolytic removal of aberrantly folded proteins that accumulate in this organelle. We used genetic and biochemical methods to analyse the involvement of N-glycosylation in the degradation...
Gespeichert in:
| Hauptverfasser: | , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
30 September 1996
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| In: |
Yeast
Year: 1996, Jahrgang: 12, Heft: 12, Pages: 1229-1238 |
| ISSN: | 1097-0061 |
| Online-Zugang: | Verlag, kostenfrei, Volltext: http://onlinelibrary.wiley.com/doi/10.1002/(SICI)1097-0061(19960930)12:12%3C1229::AID-YEA15%3E3.0.CO;2-H/abstract
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| Verfasserangaben: | Michael Knop, Nicole Hauser and Dieter H. Wolf |
MARC
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| 245 | 1 | 0 | |a N-Glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast |c Michael Knop, Nicole Hauser and Dieter H. Wolf |
| 264 | 1 | |c 30 September 1996 | |
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| 520 | |a The endoplasmic reticulum (ER) of eukaryotic cells contains a quality control system, that is required for the proteolytic removal of aberrantly folded proteins that accumulate in this organelle. We used genetic and biochemical methods to analyse the involvement of N-glycosylation in the degradation of a mutant derivative of carboxypeptidase yscY in the ER of the yeast Saccharomyces cerevisiae. Our results demonstrate that N-glycosylation of this protein is required for its degradation since an unglycosylated species is retained stably in the ER. Cells that were devoid of the ER-processing alpha 1,2-mannosidase showed reduced degradation of the glycosylated substrate protein. Disruption of CNE1, a gene encoding a putative yeast homologue for calnexin, did not exhibit any effects on the degradation of this substrate protein in vivo. Also, the alpha 1,2-mannosidase-dependent reduction in the degradation rate did not show any correlation with the function of the CNE1 gene product. Our results suggest that the ER of yeast contains a glycosylation-dependent quality control system, as has been shown for higher eukaryotic cells. | ||
| 650 | 4 | |a Saccharomyces cerevisiae | |
| 650 | 4 | |a Saccharomyces cerevisiae Proteins | |
| 650 | 4 | |a Mutation | |
| 650 | 4 | |a Calcium-Binding Proteins | |
| 650 | 4 | |a Calnexin | |
| 650 | 4 | |a Carboxypeptidases | |
| 650 | 4 | |a Cathepsin A | |
| 650 | 4 | |a Endoplasmic Reticulum | |
| 650 | 4 | |a Enzyme Stability | |
| 650 | 4 | |a Gene Deletion | |
| 650 | 4 | |a Glycosylation | |
| 650 | 4 | |a Mannosidases | |
| 650 | 4 | |a Protein Folding | |
| 700 | 1 | |a Hauser, Nicole |d 1967- |e VerfasserIn |0 (DE-588)123039975 |0 (DE-627)706137558 |0 (DE-576)184015634 |4 aut | |
| 700 | 1 | |a Wolf, Dieter H. |d 1941- |e VerfasserIn |0 (DE-588)1032061839 |0 (DE-627)737908246 |0 (DE-576)379795736 |4 aut | |
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