N-Glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast

• Verfasst von: Knop, Michael [VerfasserIn]
• Verfasst von: Hauser, Nicole [VerfasserIn]
• Verfasst von: Wolf, Dieter H. [VerfasserIn]
• Titel: N-Glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast
• Verf.angabe: Michael Knop, Nicole Hauser and Dieter H. Wolf
• Umfang: 10 S.
• Fussnoten: Gesehen am 31.08.2017 ; DOI funktioniert nicht, 31.08.2017
• Titel Quelle: Enthalten in: Yeast
• Jahr Quelle: 1996
• Band/Heft Quelle: 12(1996), 12, S. 1229-1238
• ISSN Quelle: 1097-0061
• DOI: doi:10.1002/(SICI)1097-0061(19960930)12:12<1229¬AID-YEA15>3.0.CO;2-H
• Datenträger: Online-Ressource
• Sprache: eng
• K10plus-PPN: 1562960342

Abstract

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.