title: 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.
authors.affiliation: Department of Biochemistry and Molecular Biology, Program in Molecular and Cellular Biology, University of Massachusetts, Amherst, MA, 01003, USA.
authors.forename: Lydia
authors.initials: L
authors.lastname: Lamriben
authors.affiliation: Department of Biochemistry and Molecular Biology, Program in Molecular and Cellular Biology, University of Massachusetts, Amherst, MA, 01003, USA.
authors.forename: Jill B
authors.initials: JB
authors.lastname: Graham
authors.affiliation: Department of Biochemistry and Molecular Biology, Program in Molecular and Cellular Biology, University of Massachusetts, Amherst, MA, 01003, USA.
authors.forename: Benjamin M
authors.initials: BM
authors.lastname: Adams
authors.affiliation: Department of Biochemistry and Molecular Biology, Program in Molecular and Cellular Biology, University of Massachusetts, Amherst, MA, 01003, USA.
authors.forename: Daniel N
authors.initials: DN
authors.lastname: Hebert
mesh_terms: D000818:Animals; D037281:Calnexin / Q000378:metabolism*; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006801:Humans; D018832:Molecular Chaperones / Q000378:metabolism*; D011134:Polysaccharides / Q000378:metabolism*; D011485:Protein Binding; D056811:Unfolded Protein Response
chemical_list: D018832:Molecular Chaperones; D011134:Polysaccharides; D037281:Calnexin
keywords: N-glycans; endoplasmic reticulum; molecular chaperones; protein folding; quality control