Human nuclear clusterin mediates apoptosis by interacting with Bcl-XL through C-terminal coiled coil domain |
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Authors: | Kim Nayoung Yoo Jae Cheal Han Jae Yoon Hwang Eun Mi Kim Yoon Sook Jeong Eun Young Sun Choong-Hyun Yi Gwan-Su Roh Gu Seob Kim Hyun Joon Kang Sang Soo Cho Gyeong Jae Park Jae-Yong Choi Wan Sung |
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Institution: | Department of Anatomy and Neurobiology, Medical Research Center for Neural Dysfunction, School of Medicine, Gyeongsang National University, Jinju, Gyeongnam, South Korea. |
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Abstract: | Clusterin (CLU), a glycoprotein, is involved in apoptosis, producing two alternatively spliced isoforms in various cell types. The pro-apoptotic CLU appears to be a nuclear isoform (nuclear clusterin; nCLU), and the secretory CLU (sCLU) is thought to be anti-apoptotic. The detailed molecular mechanism of nCLU as a pro-apoptotic molecule has not yet been clear. In the current study, overexpressed nCLU induced apoptosis in human kidney cells. Biochemical studies revealed that nCLU sequestered Bcl-XL via a putative BH3 motif in the C-terminal coiled coil (CC2) domain, releasing Bax, and promoted apoptosis accompanied by activation of caspase-3 and cytochrome c release. These results suggest a novel mechanism of apoptosis mediated by nCLU as a pro-apoptotic molecule. |
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Keywords: | clusterin apoptosis Bcl‐XL |
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