N‐Glycan‐based ER Molecular Chaperone and Protein Quality Control System: The Calnexin Binding Cycle

Abstract

Helenius and colleagues proposed over 20‐years ago a paradigm‐shifting model for how chaperone binding in the endoplasmic reticulum was mediated and controlled for a new type of molecular chaperone‐ the carbohydrate‐binding chaperones, calnexin and calreticulin. While the originally established basics for this lectin chaperone binding cycle holds true today, there has been a number of important advances that have expanded our understanding of its mechanisms of action, role in protein homeostasis, and its connection to disease states that are highlighted in this review.