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Pathogenic Hijacking of ER-Associated Degradation: Is ERAD Flexible?

Authors
  • Morito, Daisuke1
  • Nagata, Kazuhiro2
  • 1 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. , (Japan)
  • 2 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: [email protected] , (Japan)
Type
Published Article
Journal
Molecular cell
Publication Date
Aug 06, 2015
Volume
59
Issue
3
Pages
335–344
Identifiers
DOI: 10.1016/j.molcel.2015.06.010
PMID: 26253026
Source
Medline
License
Unknown

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.

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