Journal
SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY
Volume 41, Issue -, Pages 79-89Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.semcdb.2014.12.001
Keywords
Endoplasmic reticulum; N-glycosylation; Protein folding and quality control; Calnexin; Calreticulin; UDP-glucose glycoprotein glucosyltransferase 1
Categories
Funding
- Foundation for Research on Neurodegenerative Diseases
- Swiss National Science Foundation
- Gelu Foundation
- National Institutes of Health [GM086874, GM094848]
- Chemistry-Biology Interface program training grant [T32 GM08515]
- Comel Foundation
- Gabriele Foundation
Ask authors/readers for more resources
Asparagine-linked glycans (N-glycans) are displayed on the majority of proteins synthesized in the endoplasmic reticulum (ER). Removal of the outermost glucose residue recruits the lectin chaperone malectin possibly involved in a first triage of defective polypeptides. Removal of a second glucose promotes engagement of folding and quality control machineries built around the ER lectin chaperones calnexin (CNX) and calreticulin (CRT) and including oxidoreductases and peptidyl-prolyl isomerases. Deprivation of the last glucose residue dictates the release of N-glycosylated polypeptides from the lectin chaperones. Correctly folded proteins are authorized to leave the ER. Non-native polypeptides are recognized by the ER quality control key player UDP-glucose glycoprotein glucosyltransferase 1 (UGT1), re-glucosylated and re-addressed to the CNX/CRT chaperone binding cycle to provide additional opportunity for the protein to fold in the ER. Failure to attain the native structure determines the selection of the misfolded polypeptides for proteasome-mediated degradation. (C) 2014 Elsevier Ltd. All rights reserved.
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