title: ER chaperones in neurodegenerative disease: Folding and beyond.
abstract: Proteins along the secretory pathway are co-translationally translocated into the lumen of the endoplasmic reticulum (ER) as unfolded polypeptide chains. Afterwards, they are usually modified with N-linked glycans, correctly folded and stabilized by disulfide bonds. ER chaperones and folding enzymes control these processes. The accumulation of unfolded proteins in the ER activates a signaling response, termed the unfolded protein response (UPR). The hallmark of this response is the coordinated transcriptional up-regulation of ER chaperones and folding enzymes. In order to discuss the importance of the proper folding of certain substrates we will address the role of ER chaperones in normal physiological conditions and examine different aspects of its contribution in neurodegenerative disease. This article is part of a Special Issue entitled SI:ER stress.
authors.affiliation: Biomedical Neuroscience Institute, Faculty of Medicine, University of Chile, Santiago, Chile; Center for Geroscience, Brain Health and Metabolism, Santiago, Chile; Program of Cellular and Molecular Biology, Center for Molecular Studies of the Cell Institute of Biomedical Sciences, University of Chile, Santiago, Chile.
authors.forename: Paula
authors.initials: P
authors.lastname: Garcia-Huerta
authors.affiliation: Biomedical Neuroscience Institute, Faculty of Medicine, University of Chile, Santiago, Chile; Center for Geroscience, Brain Health and Metabolism, Santiago, Chile; Program of Cellular and Molecular Biology, Center for Molecular Studies of the Cell Institute of Biomedical Sciences, University of Chile, Santiago, Chile.
authors.forename: Leslie
authors.initials: L
authors.lastname: Bargsted
authors.affiliation: Biomedical Neuroscience Institute, Faculty of Medicine, University of Chile, Santiago, Chile; Center for Geroscience, Brain Health and Metabolism, Santiago, Chile; Program of Cellular and Molecular Biology, Center for Molecular Studies of the Cell Institute of Biomedical Sciences, University of Chile, Santiago, Chile.
authors.forename: Alexis
authors.initials: A
authors.lastname: Rivas
authors.affiliation: Neurounion Biomedical Foundation, Santiago, Chile; Biomedical Neuroscience Institute, Faculty of Medicine, University of Chile, Santiago, Chile; CENPAR, Santiago, Chile; Center for Geroscience, Brain Health and Metabolism, Santiago, Chile. Electronic address: soledad.matus@neurounion.com.
authors.forename: Soledad
authors.initials: S
authors.lastname: Matus
authors.affiliation: Neurounion Biomedical Foundation, Santiago, Chile; Biomedical Neuroscience Institute, Faculty of Medicine, University of Chile, Santiago, Chile; CENPAR, Santiago, Chile; Center for Geroscience, Brain Health and Metabolism, Santiago, Chile. Electronic address: rene.vidal@neurounion.com.
authors.forename: Rene L
authors.initials: RL
authors.lastname: Vidal
mesh_terms: D000818:Animals; D004721:Endoplasmic Reticulum / Q000378:metabolism; D059865:Endoplasmic Reticulum Stress / Q000502:physiology; D006801:Humans; D018832:Molecular Chaperones / Q000378:metabolism*; D019636:Neurodegenerative Diseases / Q000378:metabolism* / Q000473:pathology; D000074702:Proteostasis; D056811:Unfolded Protein Response / Q000502:physiology*; D015854:Up-Regulation / Q000502:physiology
chemical_list: D018832:Molecular Chaperones
keywords: ER chaperones; ER stress; Neurodegenerative disease; Protein aggregation; UPR