کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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2204897 | 1100840 | 2009 | 7 صفحه PDF | دانلود رایگان |
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.
Journal: - Volume 19, Issue 8, August 2009, Pages 357–363