title: Pathogenic Hijacking of ER-Associated Degradation: Is ERAD Flexible?
abstract: ER-associated degradation (ERAD) is a protein clearance mechanism by which misfolded, misassembled, or metabolically regulated proteins are specifically dislocated from the ER into the cytosol and degraded by the ubiquitin proteasome system. ERAD very likely evolved to maintain proteostasis and sterol homeostasis in the ER. However, the ironic truth is that membrane-penetrating transportation and protein degradation machineries in ERAD are preferably hijacked by exogenous pathogens such as viruses and toxins for their invasion and evasion from immunological surveillance. In this Review, we provide an overview of our current understanding of the pathogenic hijacking of the host cell ERAD, in which pathogens exploit the complex ERAD machinery in a variety of manners for their own use, suggesting flexibility and plasticity of the molecular machinery of ERAD.
authors.affiliation: Laboratory of Molecular and Cellular Biology, Faculty of Life Sciences, Kyoto Sangyo University, Kyoto 603-8555, Japan; CREST, Japan Science and Technology Agency, Saitama 332-0012, Japan.
authors.forename: Daisuke
authors.initials: D
authors.lastname: Morito
authors.affiliation: Laboratory of Molecular and Cellular Biology, Faculty of Life Sciences, Kyoto Sangyo University, Kyoto 603-8555, Japan; CREST, Japan Science and Technology Agency, Saitama 332-0012, Japan. Electronic address: nagata@cc.kyoto-su.ac.jp.
authors.forename: Kazuhiro
authors.initials: K
authors.lastname: Nagata
mesh_terms: D000818:Animals; D003600:Cytosol / Q000378:metabolism; D004721:Endoplasmic Reticulum / Q000378:metabolism; D060746:Endoplasmic Reticulum-Associated Degradation; D006801:Humans; D011506:Proteins / Q000737:chemistry / Q000378:metabolism; D059748:Proteolysis; D014764:Viral Proteins / Q000378:metabolism*; D014777:Virus Diseases / Q000473:pathology / Q000821:virology; D014780:Viruses / Q000378:metabolism*
chemical_list: D011506:Proteins; D014764:Viral Proteins