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• W2007025936 abstract "Proteins of the endomembrane system undergo assisted folding in the endoplasmic reticulum (ER), then quality-control and, if misfolded, ER-associated degradation (ERAD). Recent findings on the biogenesis of a type-I membrane protein (an LRP6 mutant) lead us to hypothesize the existence of a novel mechanism promoting folding of membrane proteins from the cytosolic side of the ER. The proposed folding mechanism involves cycles of chaperone binding through mono-ubiquitylation and de-ubiquitylation, followed eventually by poly-ubiquitylation and ERAD. This suggests a novel dual role for ubiquitylation in the ER – dependent on the type of ubiquitin chains involved – in folding and in degradation, and highlights the potential importance of de-ubiquitylating enzymes. Proteins of the endomembrane system undergo assisted folding in the endoplasmic reticulum (ER), then quality-control and, if misfolded, ER-associated degradation (ERAD). Recent findings on the biogenesis of a type-I membrane protein (an LRP6 mutant) lead us to hypothesize the existence of a novel mechanism promoting folding of membrane proteins from the cytosolic side of the ER. The proposed folding mechanism involves cycles of chaperone binding through mono-ubiquitylation and de-ubiquitylation, followed eventually by poly-ubiquitylation and ERAD. This suggests a novel dual role for ubiquitylation in the ER – dependent on the type of ubiquitin chains involved – in folding and in degradation, and highlights the potential importance of de-ubiquitylating enzymes." @default.
• W2007025936 created "2016-06-24" @default.
• W2007025936 creator A5073688967 @default.
• W2007025936 creator A5091422283 @default.
• W2007025936 date "2009-08-01" @default.
• W2007025936 modified "2023-10-17" @default.
• W2007025936 title "Novel ubiquitin-dependent quality control in the endoplasmic reticulum" @default.
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• W2007025936 doi "https://doi.org/10.1016/j.tcb.2009.05.005" @default.
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