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...
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| Main Authors: | , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
30 September 1996
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| In: |
Yeast
Year: 1996, Volume: 12, Issue: 12, Pages: 1229-1238 |
| ISSN: | 1097-0061 |
| Online Access: | 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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| Author Notes: | Michael Knop, Nicole Hauser and Dieter H. Wolf |
| Summary: | 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. |
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| Item Description: | Gesehen am 31.08.2017 DOI funktioniert nicht, 31.08.2017 |
| Physical Description: | Online Resource |
| ISSN: | 1097-0061 |