title: Endoplasmic reticulum-associated protein degradation--one model fits all?
abstract: The endoplasmic reticulum (ER) is the eukaryotic organelle where most secretory proteins are folded for subsequent delivery to their site of action. Proper folding of newly synthesized proteins is monitored by a stringent ER quality control system. This system recognizes misfolded or unassembled proteins and prevents them from reaching their final destination. Instead, they are extracted from the ER, polyubiquitinated and degraded by the cytosolic proteasome. With the identification of novel components and substrates, a more and more complex picture of this process emerges in which distinct pathways target different sets of substrates for destruction.
authors.affiliation: Max-Delbrück-Centrum für Molekulare Medizin, Robert-Rössle-Str. 10, 13092 Berlin, Germany.
authors.forename: Christian
authors.initials: C
authors.lastname: Hirsch
authors.forename: Ernst
authors.initials: E
authors.lastname: Jarosch
authors.forename: Thomas
authors.initials: T
authors.lastname: Sommer
authors.forename: Dieter H
authors.initials: DH
authors.lastname: Wolf
mesh_terms: D000818:Animals; D019005:Cystic Fibrosis Transmembrane Conductance Regulator / Q000502:physiology; D004721:Endoplasmic Reticulum / Q000502:physiology*; D006056:Golgi Apparatus / Q000502:physiology*; D006801:Humans; D021381:Protein Transport / Q000502:physiology; D011506:Proteins / Q000378:metabolism*; D025801:Ubiquitin / Q000502:physiology
chemical_list: C505032:CFTR protein, human; D011506:Proteins; D025801:Ubiquitin; D019005:Cystic Fibrosis Transmembrane Conductance Regulator