Next Article in Journal
Inhibition of Oral Streptococci Growth Induced by the Complementary Action of Berberine Chloride and Antibacterial Compounds
Next Article in Special Issue
Protein-Carbohydrate Interactions, and Beyond …
Previous Article in Journal
Oleanolic Acid, a Compound Present in Grapes and Olives, Protects against Genotoxicity in Human Mammary Epithelial Cells
Previous Article in Special Issue
Molecular Cloning, Carbohydrate Specificity and the Crystal Structure of Two Sclerotium rolfsii Lectin Variants
Article Menu

Export Article

Open AccessReview
Molecules 2015, 20(8), 13689-13704; doi:10.3390/molecules200813689

Glycoprotein Quality Control and Endoplasmic Reticulum Stress

Department of Biochemistry, University of Alberta, Edmonton, AB T6G 2H7, Canada
*
Author to whom correspondence should be addressed.
Academic Editor: Els Van Damme
Received: 27 April 2015 / Revised: 22 July 2015 / Accepted: 24 July 2015 / Published: 28 July 2015
(This article belongs to the Special Issue Protein-Carbohydrate Interactions, and Beyond)
View Full-Text   |   Download PDF [1101 KB, uploaded 28 July 2015]   |  

Abstract

The endoplasmic reticulum (ER) supports many cellular processes and performs diverse functions, including protein synthesis, translocation across the membrane, integration into the membrane, folding, and posttranslational modifications including N-linked glycosylation; and regulation of Ca2+ homeostasis. In mammalian systems, the majority of proteins synthesized by the rough ER have N-linked glycans critical for protein maturation. The N-linked glycan is used as a quality control signal in the secretory protein pathway. A series of chaperones, folding enzymes, glucosidases, and carbohydrate transferases support glycoprotein synthesis and processing. Perturbation of ER-associated functions such as disturbed ER glycoprotein quality control, protein glycosylation and protein folding results in activation of an ER stress coping response. Collectively this ER stress coping response is termed the unfolded protein response (UPR), and occurs through the activation of complex cytoplasmic and nuclear signaling pathways. Cellular and ER homeostasis depends on balanced activity of the ER protein folding, quality control, and degradation pathways; as well as management of the ER stress coping response. View Full-Text
Keywords: endoplasmic reticulum; calnexin; calreticulin; chaperone; stress endoplasmic reticulum; calnexin; calreticulin; chaperone; stress
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Wang, Q.; Groenendyk, J.; Michalak, M. Glycoprotein Quality Control and Endoplasmic Reticulum Stress. Molecules 2015, 20, 13689-13704.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]

Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top