منابع مشابه
Lipid disequilibrium disrupts ER proteostasis by impairing ERAD substrate glycan trimming and dislocation
The endoplasmic reticulum (ER) mediates the folding, maturation, and deployment of the secretory proteome. Proteins that fail to achieve their native conformation are retained in the ER and targeted for clearance by ER-associated degradation (ERAD), a sophisticated process that mediates the ubiquitin-dependent delivery of substrates to the 26S proteasome for proteolysis. Recent findings indicat...
متن کاملEDEM2 initiates mammalian glycoprotein ERAD by catalyzing the first mannose trimming step
Glycoproteins misfolded in the endoplasmic reticulum (ER) are subjected to ER-associated glycoprotein degradation (gpERAD) in which Htm1-mediated mannose trimming from the oligosaccharide Man8GlcNAc2 to Man7GlcNAc2 is the rate-limiting step in yeast. In contrast, the roles of the three Htm1 homologues (EDEM1/2/3) in mammalian gpERAD have remained elusive, with a key controversy being whether ED...
متن کاملTrimming
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متن کاملSweet bays of ERAD.
Proteins that improperly mature in the endoplasmic reticulum (ER) are dislocated to the cytoplasm for proteasome-mediated destruction. A recent study provides insight into the incompletely understood processes for selection and targeting of aberrant proteins for ER-associated protein degradation. The identification of the ER chaperones GRP94 and BiP as binding partners for the mannose-binding p...
متن کاملERAD substrates: which way out?
Global folding of polypeptides entering the endoplasmic reticulum (ER) starts as soon as they emerge from the narrow Sec61 translocon. Attainment of the native structure can take from several minutes to hours, depending on the gene product. Until then, non-native folding intermediates must be protected from molecular chaperones that recognize misfolded determinants and could prematurely interru...
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ژورنال
عنوان ژورنال: Journal of Cell Biology
سال: 2006
ISSN: 1540-8140,0021-9525
DOI: 10.1083/jcb.1747iti1