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http://dx.doi.org/10.5352/JLS.2015.25.4.473

Molecular Mechanism of Endoplasmic Reticulum Stress Transducer OASIS Family  

Kwon, Kisang (Department of Biomedical Laboratory Science, College of Health & Welfare, Kyungwoon University)
Kim, Seung-Whan (Department of Emergency Medicine, Chungnam National University Hospital)
Yu, Kweon (Korea Research Institute of Bioscience & Biotechnology)
Kwon, O-Yu (Department of Anatomy, College of Medicine, Chungnam National University)
Publication Information
Journal of Life Science / v.25, no.4, 2015 , pp. 473-480 More about this Journal
Abstract
The endoplasmic reticulum (ER) in the eukaryotic cells is the first compartment in the secretory pathway. Almost secretory proteins and membrane proteins are secreted through the ER, in which post-translational modifications occur via diverse signals from the ER lumen to the cytoplasm and nucleus. Only then are correctly-folded proteins secreted to the outside cells. Unfolded proteins that accumulate in the ER cause a kind of intracellular stress, ER stress, and activate an unfolded protein response (UPR) system. The 3 major transducers of the UPR are inositol requiring 1 (IRE1), PKR-like ER kinase (PERK) and activating transcription factor 6 (ATF6), all of which are ER transmembrane proteins. Recently, novel types of a new ATF6 family have been identified. Those commonly have an ER-transmembrane domain, a transcription-activation domain and a basic leucine zipper (bZIP) domain―Luman, OASIS, BBF2H7, CREBH and CREB4. Each factor functions by regulating the UPR in specific organs and tissues. Although the detailed molecular mechanisms of OASIS family members are unknown, in this study we comprehensively introduce these molecular signals.
Keywords
Endoplasmic reticulum (ER); old astrocyte specifically induced substance (OASIS); unfolded protein response (UPR);
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