Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 44, Issue 10, Pages 827-836Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2019.04.012
Keywords
-
Categories
Funding
- Israel Science Foundation [1593/16]
Ask authors/readers for more resources
The ability of mammalian cells to correctly identify and degrade misfolded secretory proteins, most of them bearing N-glycans, is crucial for their correct function and survival. An inefficient disposal mechanism results in the accumulation of misfolded proteins and consequent endoplasmic reticulum (ER) stress. N-glycan processing creates a code that reveals the folding status of each molecule, enabling continued folding attempts or targeting of the doomed glycoprotein for disposal. We review here the main steps involved in the accurate processing of unfolded glycoproteins. We highlight recent data suggesting that the processing is not stochastic, but that there is selective accelerated glycan trimming on misfolded glycoprotein molecules.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available