ER Quality Control: The Cytoplasmic Connection

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ER Quality Control: The Cytoplasmic Connection

unfolded substrate into the active site. Proteasomes The endoplasmic reticulum (ER) is the port of entry of are abundant in the cytoplasm and nucleus, but are membrane and secretory proteins into the central vacuapparently absent from the ER lumen. olar system, which includes the ER itself, the Golgi appaMutations in the cystic fibrosis transmembrane conratus, lysosomes, endosomes, the plasma m...

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The ER glycoprotein quality control system.

The endoplasmic reticulum (ER) is the major site for folding and sorting of newly synthesized secretory cargo proteins. One central regulator of this process is the quality control machinery, which retains and ultimately disposes of misfolded secretory proteins before they can exit the ER. The ER quality control process is highly effective and mutations in cargo molecules are linked to a variet...

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A Role for Macro-ER-Phagy in ER Quality Control

The endoplasmic-reticulum quality-control (ERQC) system shuttles misfolded proteins for degradation by the proteasome through the well-defined ER-associated degradation (ERAD) pathway. In contrast, very little is known about the role of autophagy in ERQC. Macro-autophagy, a collection of pathways that deliver proteins through autophagosomes (APs) for degradation in the lysosome (vacuole in yeas...

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N-glycan processing in ER quality control.

Glycosylation of asparagine residues in Asn-x-Ser/Thr motifs is a common covalent modification of proteins in the lumen of the endoplasmic reticulum (ER). By substantially contributing to the overall hydrophilicity of the polypeptide, pre-assembled core glycans inhibit possible aggregation caused by the inevitable exposure of hydrophobic patches on the as yet unstructured chains. Thereafter, N-...

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Protein maturation in the endoplasmic reticulum (ER) is subject to stringent quality control. Terminally misfolded polypeptides are usually ejected into the cytoplasm and targeted for destruction by the proteasome. Ubiquitin conjugation is essential for both extraction and proteolysis. We discuss the role of the ubiquitin conjugation machinery in this pathway and focus on the role of ubiquitin ...

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ژورنال

عنوان ژورنال: Cell

سال: 1997

ISSN: 0092-8674

DOI: 10.1016/s0092-8674(00)81881-4