Autophagy: an ER Protein Quality Control Process
نویسندگان
چکیده
منابع مشابه
Protein O-mannosyltransferases participate in ER protein quality control.
In eukaryotic cells, proteins enter the secretory pathway at the endoplasmic reticulum (ER) as linear polypeptides and fold after translocation across or insertion into the membrane. If correct folding fails, many proteins are O-mannosylated inside the ER by an O-mannosyltransferase, the Pmt1p-Pmt2p complex. The consequences of this modification are controversial and the cellular role of the Pm...
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Even with the assistance of many cellular factors, a significant fraction of newly synthesized proteins ends up misfolded. Cells evolved protein quality control systems to ensure that these potentially toxic species are detected and eliminated. The best characterized of these pathways, the ER-associated protein degradation (ERAD), monitors the folding of membrane and secretory proteins whose bi...
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The endoplasmic reticulum (ER) uses an elaborate surveillance system called the ER quality control (ERQC) system. The ERQC facilitates folding and modification of secretory and membrane proteins and eliminates terminally misfolded polypeptides through ER-associated degradation (ERAD) or autophagic degradation. This mechanism of ER protein surveillance is closely linked to redox and calcium home...
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Protein degradation constitutes a central pillar in proteome maintenance. In eukaryotes, specific protein turnover is predominantly achieved by the ubiquitinproteasome system (UPS). Therein, substrate proteins are first covalently decorated with the small protein ubiquitin. Sequential addition of ubiquitin monomers results in a polyubiquitin chain on a substrate, the signal for proteasomal degr...
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ژورنال
عنوان ژورنال: Autophagy
سال: 2006
ISSN: 1554-8627,1554-8635
DOI: 10.4161/auto.2.2.2388