Polyglutamine expansion disturbs the endoplasmic reticulum formation, leading to caspase-7 activation through Bax
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- 作者：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
- 关键词：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
- 刊名：Biochemical and Biophysical Research Communications
- 出版年：24 January, 2014
- 年：2014
- 卷：443
- 期：4
- 页码：1232-1238
- 全文大小：1702 K
文摘
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鈥檚 disease. We can conclude that polyglutamine expansion may drive caspase-7 activation by disrupting the ER membrane.