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Science 5 December 1997:
Vol. 278. no. 5344, pp. 1806 - 1809
DOI: 10.1126/science.278.5344.1806
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Reports

Role of Cue1p in Ubiquitination and Degradation at the ER Surface

Thomas Biederer, Corinna Volkwein, Thomas Sommer *

Endoplasmic reticulum (ER) degradation of aberrant proteins is mediated by the ubiquitin-proteasome pathway. Here, a membrane-bound component of the ubiquitin system, Cue1p, was identified. It was shown to recruit the soluble ubiquitin-conjugating enzyme Ubc7p to the ER membrane. In the absence of Cue1p, unassembled and thus cytosolically mislocalized Ubc7p was unable to participate in ER degradation or in the turnover of soluble non-ER proteins. Moreover, ubiquitination by Cue1p-assembled Ubc7p and Ubc6p was a prerequisite for retrograde transport of lumenal substrates out of the ER, which suggests that ubiquitination is mechanistically integrated into the ER degradation process.

Max-Delbrück Center for Molecular Medicine, Robert-Rössle-Strasse 10, 13122 Berlin, Germany.
*   To whom correspondence should be addressed. E-mail: tsommer{at}mdc-berlin.de

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J. Cell Sci. 111, 2217-2226
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Endoplasmic Reticulum (ER)-associated Degradation of Misfolded N-Linked Glycoproteins Is Suppressed upon Inhibition of ER Mannosidase I.
F. Tokunaga, C. Brostrom, T. Koide, and P. Arvan (2000)
J. Biol. Chem. 275, 40757-40764
   Abstract »    Full Text »    PDF »
The Amino-terminal Domain of Apolipoprotein B Does Not Undergo Retrograde Translocation from the Endoplasmic Reticulum to the Cytosol. PROTEASOMAL DEGRADATION OF NASCENT APOLIPOPROTEIN B BEGINS AT THE CARBOXYL TERMINUS OF THE PROTEIN, WHILE APOLIPOPROTEIN B IS STILL IN ITS ORIGINAL TRANSLOCON.
J.-s. Liang, X. Wu, E. A. Fisher, and H. N. Ginsberg (2000)
J. Biol. Chem. 275, 32003-32010
   Abstract »    Full Text »    PDF »
Ubiquitin-mediated Proteolysis of a Short-lived Regulatory Protein Depends on Its Cellular Localization.
U. Lenk and T. Sommer (2000)
J. Biol. Chem. 275, 39403-39410
   Abstract »    Full Text »    PDF »
Newly Synthesized Human delta Opioid Receptors Retained in the Endoplasmic Reticulum Are Retrotranslocated to the Cytosol, Deglycosylated, Ubiquitinated, and Degraded by the Proteasome.
U. E. Petaja-Repo, M. Hogue, A. Laperriere, S. Bhalla, P. Walker, and M. Bouvier (2001)
J. Biol. Chem. 276, 4416-4423
   Abstract »    Full Text »    PDF »
Endoplasmic Reticulum (ER)-associated Degradation of T Cell Receptor Subunits. INVOLVEMENT OF ER-ASSOCIATED UBIQUITIN-CONJUGATING ENZYMES (E2s).
S. Tiwari and A. M. Weissman (2001)
J. Biol. Chem. 276, 16193-16200
   Abstract »    Full Text »    PDF »
Co-translational Interactions of Apoprotein B with the Ribosome and Translocon during Lipoprotein Assembly or Targeting to the Proteasome.
R. Pariyarath, H. Wang, J. D. Aitchison, H. N. Ginsberg, W. J. Welch, A. E. Johnson, and E. A. Fisher (2001)
J. Biol. Chem. 276, 541-550
   Abstract »    Full Text »    PDF »
Membrane Topology and Function of Der3/Hrd1p as a Ubiquitin-Protein Ligase (E3) Involved in Endoplasmic Reticulum Degradation.
P. M. Deak and D. H. Wolf (2001)
J. Biol. Chem. 276, 10663-10669
   Abstract »    Full Text »    PDF »
The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum.
S. Fang, M. Ferrone, C. Yang, J. P. Jensen, S. Tiwari, and A. M. Weissman (2001)
PNAS 98, 14422-14427
   Abstract »    Full Text »    PDF »


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