ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway
In: Science (New York, N.Y.), Jg. 273 (1996-09-20), Heft 5282
Online
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Zugriff:
Secretion of proteins is initiated by their uptake into the endoplasmic reticulum (ER), which possesses a proteolytic system able to degrade misfolded and nonassembled proteins. The ER degradation system was studied with yeast mutants defective in the breakdown of a mutated soluble vacuolar protein, carboxypeptidase yscY (CPY*). The ubiquitin-conjugating enzyme Ubc7p participated in the degradation process, which was mediated by the cytosolic 26S proteasome. It is likely that CPY* entered the ER, was glycosylated, and was then transported back out of the ER lumen to the cytoplasmic side of the organelle, where it was conjugated with ubiquitin and degraded.
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ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway
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Autor/in / Beteiligte Person: | Wolf, Dieter H. ; Schweiger, Markus ; Hiller, Mark M. ; Finger, Andreas |
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Zeitschrift: | Science (New York, N.Y.), Jg. 273 (1996-09-20), Heft 5282 |
Veröffentlichung: | 1996 |
Medientyp: | unknown |
ISSN: | 0036-8075 (print) |
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