A membrane protein required for dislocation of misfolded proteins from the ER.Approximately 25% of eukaryotic genes code for integral membrane proteins that are assembled at the endoplasmic reticulum. The pathway of US11-dependent degradation of MHC class I heavy chains involves a ubiquitin-conjugated intermediate. An integrated stress response regulates amino acid metabolism and resistance to oxidative stress. A survival pathway for Caenorhabditis elegans with a blocked unfolded protein response. Ingestion of bacterially expressed dsRNAs can produce specific and potent genetic interference in Caenorhabditis elegans. Reconstitution of membrane proteolysis by FtsH. Regulation of the selenoprotein SelS by glucose deprivation and endoplasmic reticulum stress-SelS is a novel glucose-regulated protein. Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum. The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Endoplasmic reticulum degradation requires lumen to cytosol signaling. Genetic interactions of Hrd3p and Der3p/Hrd1p with Sec61p suggest a retro-translocation complex mediating protein transport for ER degradation. IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum. Dislocation of a type I membrane protein requires interactions between membrane-spanning segments within the lipid bilayer. Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Polyubiquitin serves as a recognition signal, rather than a ratcheting molecule, during retrotranslocation of proteins across the endoplasmic reticulum membrane. Complete structure of p97/valosin-containing protein reveals communication between nucleotide domains. Characterization of mammalian selenoproteomes. 1p, a protein required for degradation of malfolded soluble proteins of the endoplasmic reticulum: topology and Der1-like proteins. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control. Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast. Knop, M., Finger, A., Braun, T., Hellmuth, K. EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin. Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle. Molinari, M., Calanca, V., Galli, C., Lucca, P. Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin. Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation. Export of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase. The cytosolic tail of class I MHC heavy chain is required for its dislocation by the human cytomegalovirus US2 and US11 gene products. Substrate recognition in ER-associated degradation mediated by Eps1, a member of the protein disulfide isomerase family. AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation. Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48. The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins. AAA proteases: cellular machines for degrading membrane proteins. Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways. Integration of endoplasmic reticulum signaling in health and disease. The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol. Retro-translocation of proteins from the endoplasmic reticulum into the cytosol. ER quality control: towards an understanding at the molecular level.
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