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Science 20 September 1996:
Vol. 273. no. 5282, pp. 1725 - 1728
DOI: 10.1126/science.273.5282.1725
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Reports

ER Degradation of a Misfolded Luminal Protein by the Cytosolic Ubiquitin-Proteasome Pathway

Mark M. Hiller, Andreas Finger, Markus Schweiger, Dieter H. Wolf *

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.

Institut für Biochemie der Universität Stuttgart, Pfaffenwaldring 55, D-70569 Stuttgart, Germany.
*   To whom correspondence should be addressed.

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Int. Immunol. 13, 249-256
   Abstract »    Full Text »    PDF »
Endoplasmic Reticulum Degradation Requires Lumen to Cytosol Signaling: Transmembrane Control of Hrd1p by Hrd3p.
R. G. Gardner, G. M. Swarbrick, N. W. Bays, S. R. Cronin, S. Wilhovsky, L. Seelig, C. Kim, and R. Y. Hampton (2000)
J. Cell Biol. 151, 69-82
   Abstract »    Full Text »    PDF »
Degradation Signals Recognized by the Ubc6p-Ubc7p Ubiquitin-Conjugating Enzyme Pair.
T. Gilon, O. Chomsky, and R. G. Kulka (2000)
Mol. Cell. Biol. 20, 7214-7219
   Abstract »    Full Text »
The Unfolded Protein Response Regulates Multiple Aspects of Secretory and Membrane Protein Biogenesis and Endoplasmic Reticulum Quality Control.
D. T.W. Ng, E. D. Spear, and P. Walter (2000)
J. Cell Biol. 150, 77-88
   Abstract »    Full Text »    PDF »
PNG1, a Yeast Gene Encoding a Highly Conserved Peptide:N-Glycanase.
T. Suzuki, H. Park, N. M. Hollingsworth, R. Sternglanz, and W. J. Lennarz (2000)
J. Cell Biol. 149, 1039-1052
   Abstract »    Full Text »    PDF »
Accelerated Proteasomal Degradation of Membrane Ig Heavy Chains.
S. C. Ho, S. Chaudhuri, A. Bachhawat, K. McDonald, and S. Pillai (2000)
J. Immunol. 164, 4713-4719
   Abstract »    Full Text »    PDF »
HRD Gene Dependence of Endoplasmic Reticulum-associated Degradation.
S. Wilhovsky, R. Gardner, and R. Hampton (2000)
Mol. Biol. Cell 11, 1697-1708
   Abstract »    Full Text »
Degradation of unassembled soluble Ig subunits by cytosolic proteasomes: evidence that retrotranslocation and degradation are coupled events.
R. MANCINI, C. FAGIOLI, A. M. FRA, C. MAGGIONI, and R. SITIA (2000)
FASEB J 14, 769-778
   Abstract »    Full Text »
Cholera Toxin Is Exported from Microsomes by the Sec61p Complex.
A. Schmitz, H. Herrgen, A. Winkeler, and V. Herzog (2000)
J. Cell Biol. 148, 1203-1212
   Abstract »    Full Text »    PDF »
Regulation of Hmg-Coa Reductase Degradation Requires the P-Type Atpase Cod1p/Spf1p.
S. R. Cronin, A. Khoury, D. K. Ferry, and R. Y. Hampton (2000)
J. Cell Biol. 148, 915-924
   Abstract »    Full Text »    PDF »
Loss of the Major Isoform of Phosphoglucomutase Results in Altered Calcium Homeostasis in Saccharomyces cerevisiae.
L. Fu, A. Miseta, D. Hunton, R. B. Marchase, and D. M. Bedwell (2000)
J. Biol. Chem. 275, 5431-5440
   Abstract »    Full Text »    PDF »
Mannose Trimming Targets Mutant alpha 2-Plasmin Inhibitor for Degradation by the Proteasome.
D. H. Chung, K. Ohashi, M. Watanabe, N. Miyasaka, and S. Hirosawa (2000)
J. Biol. Chem. 275, 4981-4987
   Abstract »    Full Text »    PDF »
Identification of a Ubiquitination-Target/Substrate-Interaction Domain of Cytochrome P-450 (CYP) 2E1.
A. Banerjee, T. A. Kocarek, and R. F. Novak (2000)
Drug Metab. Dispos. 28, 118-124
   Abstract »    Full Text »
Endocytosis and Degradation of the Growth Hormone Receptor Are Proteasome-dependent.
P. van Kerkhof, R. Govers, C. M. Alves dos Santos, and G. J. Strous (2000)
J. Biol. Chem. 275, 1575-1580
   Abstract »    Full Text »    PDF »
Distinct Domains within Yeast Sec61p Involved in Post-translational Translocation and Protein Dislocation.
B. M. Wilkinson, J. R. Tyson, P. J. Reid, and C. J. Stirling (2000)
J. Biol. Chem. 275, 521-529
   Abstract »    Full Text »    PDF »


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