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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.

SUBMITTER: Lamriben L

PROVIDER: S-EPMC4805476 | biostudies-literature | 2016 Apr

REPOSITORIES: biostudies-literature

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

Lamriben Lydia L Graham Jill B JB Adams Benjamin M BM Hebert Daniel N DN

Traffic (Copenhagen, Denmark) 20160110 4

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 ...[more]

PMID: 26676362

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