title: In and out of the ER: protein folding, quality control, degradation, and related human diseases.
abstract: A substantial fraction of eukaryotic gene products are synthesized by ribosomes attached at the cytosolic face of the endoplasmic reticulum (ER) membrane. These polypeptides enter cotranslationally in the ER lumen, which contains resident molecular chaperones and folding factors that assist their maturation. Native proteins are released from the ER lumen and are transported through the secretory pathway to their final intra- or extracellular destination. Folding-defective polypeptides are exported across the ER membrane into the cytosol and destroyed. Cellular and organismal homeostasis relies on a balanced activity of the ER folding, quality control, and degradation machineries as shown by the dozens of human diseases related to defective maturation or disposal of individual polypeptides generated in the ER.
authors.affiliation: Department of Biochemistry and Molecular Biology, Program in Molecular and Cellular Biology, University of Massachusetts, Amherst, Massachusetts 01003, USA. dehebert@biochem.umass.edu
authors.forename: Daniel N
authors.initials: DN
authors.lastname: Hebert
authors.forename: Maurizio
authors.initials: M
authors.lastname: Molinari
mesh_terms: D004721:Endoplasmic Reticulum / Q000502:physiology*; D006801:Humans; D008659:Metabolic Diseases / Q000209:etiology* / Q000503:physiopathology; D018832:Molecular Chaperones / Q000502:physiology; D014176:Protein Biosynthesis / Q000502:physiology; D017510:Protein Folding
chemical_list: D018832:Molecular Chaperones