title: The activities and function of molecular chaperones in the endoplasmic reticulum.
abstract: Most proteins in the secretory pathway are translated, folded, and subjected to quality control at the endoplasmic reticulum (ER). These processes must be flexible enough to process diverse protein conformations, yet specific enough to recognize when a protein should be degraded. Molecular chaperones are responsible for this decision making process. ER associated chaperones assist in polypeptide translocation, protein folding, and ER associated degradation (ERAD). Nevertheless, we are only beginning to understand how chaperones function, how they are recruited to specific substrates and assist in folding/degradation, and how unique chaperone classes make quality control "decisions".
authors.affiliation: Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, United States. teb20@pitt.edu
authors.forename: Teresa M
authors.initials: TM
authors.lastname: Buck
authors.forename: Christine M
authors.initials: CM
authors.lastname: Wright
authors.forename: Jeffrey L
authors.initials: JL
authors.lastname: Brodsky
mesh_terms: D004721:Endoplasmic Reticulum; D018832:Molecular Chaperones / Q000378:metabolism / Q000502:physiology*; D011489:Protein Denaturation; D017510:Protein Folding; D021381:Protein Transport
chemical_list: D018832:Molecular Chaperones