ER Stress and Disease: Toward Prevention and Treatment

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  • Kaneko Masayuki
    Department of Biochemistry, Institute of Biomedical and Health Sciences, Hiroshima University
  • Imaizumi Kazunori
    Department of Biochemistry, Institute of Biomedical and Health Sciences, Hiroshima University
  • Saito Atsushi
    Department of Stress Protein Processing, Institute of Biomedical and Health Sciences, Hiroshima University
  • Kanemoto Soshi
    Department of Biochemistry, Institute of Biomedical and Health Sciences, Hiroshima University
  • Asada Rie
    Department of Biochemistry, Institute of Biomedical and Health Sciences, Hiroshima University
  • Matsuhisa Koji
    Department of Stress Protein Processing, Institute of Biomedical and Health Sciences, Hiroshima University
  • Ohtake Yosuke
    Department of Biochemistry, Institute of Biomedical and Health Sciences, Hiroshima University

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<p>Secretory and membrane proteins are synthesized in ribosomes, then mature in the endoplasmic reticulum (ER), but if ER function is impaired, immature defective proteins accumulate in the ER. This situation is called ER stress: in response, a defensive mechanism called the unfolded protein response (UPR) is activated in cells to reduce the defective proteins. During the UPR, the ER transmembrane sensor molecules inositol-requiring enzyme 1 (IRE1), activating transcription factor 6 (ATF6), and RNA-dependent protein kinase (PKR)-like ER kinase (PERK) are activated, stress signals are transduced to the outside of the ER, and various cell responses, including gene induction, occur. In ER-associated degradation (ERAD), one type of UPR, defective proteins are eventually expelled from the ER and degraded in the cytoplasm through the ubiquitin proteasome system. Since ER stress has been reported to have relationships with neurodegenerative diseases, diabetes, metabolic syndromes, and cancer, it is the focus of increased attention from the perspectives of elucidating pathogenic mechanisms, and in the development of therapeutics.</p>

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