Polyglutamine expansion disturbs the endoplasmic reticulum formation,leading to caspase-7 activation through Bax |
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| Authors: | Masashi Ueda Shimo Li Masanori Itoh Yoshika Hayakawa-Yano Miao-xing Wang Miki Hayakawa Ryoko Hasebe-Matsubara Kazunori Ohta Eri Ohta Akihito Mizuno Yoko Hida Munekazu Matsumoto Huayue Chen Toshiyuki Nakagawa |
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| Institution: | 1. Department of Neurobiology, Gifu University Graduate School of Medicine, Gifu, Japan;2. Department of Anatomy, Gifu University Graduate School of Medicine, Gifu, Japan |
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| Abstract: | The endoplasmic reticulum (ER) plays a pivotal role in cellular functions such as the ER stress response. However, the effect of the ER membrane on caspase activation remains unclear. This study reveals that polyglutamine oligomers augmented at ER induce insertion of Bax into the ER membrane, thereby activating caspase-7. In line with the role of ER in cell death induced by polyglutamine expansion, the ER membrane was found to be disrupted and dilated in the brain of a murine model of Huntington’s disease. We can conclude that polyglutamine expansion may drive caspase-7 activation by disrupting the ER membrane. |
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| Keywords: | Apaf-1 Apoptotic protease activating factor 1 cb5 cytochrome b5 polyQ79 polyQ82 polyglutamine repeats containing proteins with 79 or 82 glutamine residues xbp-1 x-box binding protein 1 FRET fluorescence resonance energy transfer |
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