title: Participation of lectin chaperones and thiol oxidoreductases in protein folding within the endoplasmic reticulum.
abstract: Protein folding within the endoplasmic reticulum occurs in conjunction with a complex array of molecular chaperones and folding catalysts that assist the folding process as well as function in quality control processes to monitor the outcome. In this review, we summarize recent advances in the calnexin/calreticulin chaperone system that is directed primarily toward Asn-linked glycoproteins, as well as the protein disulfide isomerase family of enzymes that catalyze disulfide formation, reduction, and isomerization. We highlight issues related to function and substrate specificity as well as the functional interplay between the two systems.
authors.affiliation: Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada M5S 1A8.
authors.forename: Lori A
authors.initials: LA
authors.lastname: Rutkevich
authors.forename: David B
authors.initials: DB
authors.lastname: Williams
mesh_terms: D000818:Animals; D017209:Apoptosis; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006801:Humans; D037102:Lectins / Q000378:metabolism*; D018832:Molecular Chaperones / Q000378:metabolism*; D010088:Oxidoreductases / Q000378:metabolism*; D017510:Protein Folding
chemical_list: D037102:Lectins; D018832:Molecular Chaperones; D010088:Oxidoreductases