Journal ArticleDOI
ER-associated and proteasomemediated protein degradation: how two topologically restricted events came together
TLDR
A protein-degradation pathway associated with the endoplasmic reticulum (ER) can selectively remove polypeptides from the secretory pathway and recent advances in understanding how each of these steps is achieved are summarized.About:
This article is published in Trends in Cell Biology.The article was published on 1997-04-01. It has received 188 citations till now. The article focuses on the topics: Protein degradation & Endoplasmic-reticulum-associated protein degradation.read more
Citations
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Journal ArticleDOI
The Ubiquitin System
Avram Hershko,Aaron Ciechanover +1 more
TL;DR: This review discusses recent information on functions and mechanisms of the ubiquitin system and focuses on what the authors know, and would like to know, about the mode of action of ubi...
Journal ArticleDOI
The 26S Proteasome: A Molecular Machine Designed for Controlled Proteolysis
TL;DR: In eukaryotic cells, most proteins in the cytosol and nucleus are degraded via the ubiquitin-proteasome pathway, and the 26S proteasome is a 2-MDa molecular machine built from approximately 31 different subunits, which catalyzes protein degradation.
Journal ArticleDOI
Proteasome inhibitors: valuable new tools for cell biologists.
Do Hee Lee,Alfred L. Goldberg +1 more
TL;DR: The actions of selective proteasome inhibitors are described, how they can be used to investigate cellular responses, the functions of the proteasomes demonstrated by such studies and their potential applications in the future.
Journal ArticleDOI
Setting the standards: quality control in the secretory pathway.
TL;DR: Quality control improves folding efficiency by retaining proteins in the special folding environment of the endoplasmic reticulum, and it prevents harmful effects that could be caused by the deployment of incompletely folded or assembled proteins.
Journal ArticleDOI
A Novel Human WD Protein, h-βTrCP, that Interacts with HIV-1 Vpu Connects CD4 to the ER Degradation Pathway through an F-Box Motif
Florence Margottin,Stephan Bour,Hervé Durand,Luc Selig,Serge Benichou,Virginie Richard,Dominique Thomas,Klaus Strebel,Richard Benarous +8 more
TL;DR: HIV-1 Vpu interacts with CD4 in the endoplasmic reticulum and triggers CD4 degradation, presumably by proteasomes, and beta TrCP identified by interaction with Vpu connects CD4 to this proteolytic machinery, and CD4-Vpu-beta TrCP ternary complexes have been detected by coimmunoprecipitation.
References
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Journal ArticleDOI
Molecular chaperones in cellular protein folding.
TL;DR: Significant progress has been made in the understanding of the ATP-dependent mechanisms used by the Hsp70 and chaperonin families of molecular chaperones, which can cooperate to assist in folding new polypeptide chains.
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Degradation of CFTR by the ubiquitin-proteasome pathway
TL;DR: It is shown that the degradation of both wild-type and mutant CFTR is inhibited by two potent proteasome inhibitors that induce the accumulation of polyubiquitinated forms of immature CFTR, confirming that ubiquitination is required for rapid CFTR degradation.
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Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction.
Emmanuel J. H. J. Wiertz,Domenico Tortorella,Matthew Bogyo,Joyce Yu,Walther Mothes,Thomas R. Jones,Tom A. Rapoport,Hidde L. Ploegh +7 more
TL;DR: The human cytomegalovirus genome encodes proteins that trigger destruction of newly synthesized major histocompatibility complex (MHC) class I molecules, which involves the Sec6l complex, in what appears to be a reversal of the reaction by which it translocates nascent chains into the endoplasmic reticulum.
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The Human Cytomegalovirus US11 Gene Product Dislocates MHC Class I Heavy Chains from the Endoplasmic Reticulum to the Cytosol
Emmanuel J. H. J. Wiertz,Thomas R. Jones,Lei Sun,Matthew Bogyo,Hans J. Geuze,Hidde L. Ploegh +5 more
TL;DR: Human cytomegalovirus (HCMV) down-regulates expression of MHC class I products by selective proteolysis by encodes an endoplasmic reticulum resident type-I transmembrane glycoprotein, which dislocates newly synthesized class I molecules from the ER to the cytosol, where they are acted upon by an N-glycanase and the proteasome.
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Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
Timothy J. Jensen,Melinda A. Loo,Steven Pind,David B. Williams,Alfred L. Goldberg,John R. Riordan +5 more
TL;DR: It is shown that this ER degradation is sensitive to inhibitors of the cytosolic proteasome, including lactacystin and certain peptide aldehydes, which completely blocks the ATP-dependent conversion of the wild-type precursor to the native folded form that enables escape from degradation.