The action of molecular chaperones in the early secretory pathway

SW Fewell, KJ Travers, JS Weissman… - Annual review of …, 2001 - annualreviews.org
SW Fewell, KJ Travers, JS Weissman, JL Brodsky
Annual review of genetics, 2001annualreviews.org
▪ Abstract The endoplasmic reticulum (ER) serves as a way-station during the biogenesis of
nearly all secreted proteins, and associated with or housed within the ER are factors
required to catalyze their import into the ER and facilitate their folding. To ensure that only
properly folded proteins are secreted and to temper the effects of cellular stress, the ER can
target aberrant proteins for degradation and/or adapt to the accumulation of misfolded
proteins. Molecular chaperones play critical roles in each of these phenomena.
Abstract
The endoplasmic reticulum (ER) serves as a way-station during the biogenesis of nearly all secreted proteins, and associated with or housed within the ER are factors required to catalyze their import into the ER and facilitate their folding. To ensure that only properly folded proteins are secreted and to temper the effects of cellular stress, the ER can target aberrant proteins for degradation and/or adapt to the accumulation of misfolded proteins. Molecular chaperones play critical roles in each of these phenomena.
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