Title:
Roles of Endoplasmic Reticulum Stress Response Pathway in Health and Disiease

Oyadomari Seiichi, M.D., Ph.D.
Professor
Division of Molecular Biology,
Institute for Genome Research,
The University of Tokushima

曜日・時間・開場にご注意ください！　6月11日(火)　16:30～17:30　山崎記念館１階　研修ホール

Abstract:
Disruption of the folding of proteins synthesized in the endoplasmic reticulum (ER) due to various physiological or pathological conditions is known as ER stress. To adapt to ER stress, cell induces the ER stress response via a signal transduction pathway transmitted from the ER. During the ER stress, the ER stress response signal transducer proteins, ATF6, IRE1, and PERK that are present in the ER membrane and activated by ER stress, transmit three independent signals to restore the protein-folding environment in the ER by decreasing the ER protein-folding burden via translational control, increasing ER protein-folding capacity via transcriptional induction, and facilitating degradation of incompletely folded proteins.
ER plays a vital role not only in the folding of membrane and secretory proteins but also in cellular functions such as calcium storage and lipid synthesis. Factors such as calcium depletion from the ER or administration of excess fatty acids to the ER cause ER stress. Thus, ER stress response signals may be utilized in the regulation of various biological functions in addition to protein folding. Research findings in recent years have elucidated that the ER stress response regulates not only proteostasis in the ER but also biological functions, such as metabolism . innate immunity and development, which are not directly related to protein-folding quality control. Therefore, ER stress response dysfunction has been implicated in the pathogenesis of various disease including diabetes, ischemia, cancer and neurodegenerative disorders.