title: Five Questions (with their Answers) on ER-Associated Degradation.
abstract: Production of a functional proteome is a major burden for our cells. Native proteins operate inside and outside the cells to eventually warrant life and adaptation to metabolic and environmental changes, there is no doubt that production and inappropriate handling of misfolded proteins may cause severe disease states. This review focuses on protein destruction, which is, paradoxically, a crucial event for cell and organism survival. It regulates the physiological turnover of proteins and the clearance of faulty biosynthetic products. It mainly relies on the intervention of two catabolic machineries, the ubiquitin proteasome system and the (auto)lysosomal system. Here, we have selected five questions dealing with how, why and when proteins produced in the mammalian endoplasmic reticulum are eventually selected for destruction.
authors.affiliation: Institute for Research in Biomedicine, CH-6500, Bellinzona, Switzerland.|Università della Svizzera italiana, CH-6900, Lugano, Switzerland.|ETH Zurich, D-BIOL, 8093, Zurich, Switzerland.
authors.forename: Giorgia Brambilla
authors.initials: GB
authors.lastname: Pisoni
authors.affiliation: Institute for Research in Biomedicine, CH-6500, Bellinzona, Switzerland.|Università della Svizzera italiana, CH-6900, Lugano, Switzerland.|School of Life Sciences, École Polytechnique Fédérale de Lausanne (EPFL), CH-1015, Lausanne, Switzerland.
authors.forename: Maurizio
authors.initials: M
authors.lastname: Molinari
mesh_terms: D000818:Animals; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D060746:Endoplasmic Reticulum-Associated Degradation; D006801:Humans; D059748:Proteolysis
keywords: ERAD tuning; autophagy; endoplasmic reticulum-associated degradation; protein folding; protein misfolding (conformational) diseases; protein quality control; ubiquitin proteasome system; unfolded protein response