title: The endoplasmic reticulum: A hub of protein quality control in health and disease.
abstract: One third of the eukaryotic proteome is synthesized at the endoplasmic reticulum (ER), whose unique properties provide a folding environment substantially different from the cytosol. A healthy, balanced proteome in the ER is maintained by a network of factors referred to as the ER quality control (ERQC) machinery. This network consists of various protein folding chaperones and modifying enzymes, and is regulated by stress response pathways that prevent the build-up as well as the secretion of potentially toxic and aggregation-prone misfolded protein species. Here, we describe the components of the ERQC machinery, investigate their response to different forms of stress, and discuss the consequences of ERQC break-down.
authors.affiliation: Max Planck Institute of Biochemistry, Department of Cellular Biochemistry, 82152 Martinsried, Germany.
authors.forename: Lisa
authors.initials: L
authors.lastname: Vincenz-Donnelly
authors.affiliation: Max Planck Institute of Biochemistry, Department of Cellular Biochemistry, 82152 Martinsried, Germany.
authors.forename: Mark S
authors.initials: MS
authors.lastname: Hipp
mesh_terms: D000818:Animals; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D059865:Endoplasmic Reticulum Stress; D006801:Humans; D018832:Molecular Chaperones / Q000378:metabolism; D017510:Protein Folding; D021381:Protein Transport; D056811:Unfolded Protein Response
chemical_list: D018832:Molecular Chaperones
keywords: Endoplasmic reticulum; Proteostasis; Quality control