JAB1 participates in unfolded protein responses by association and dissociation with IRE1

被引:81
作者
Oono, K
Yoneda, T
Manabe, T
Yamagishi, S
Matsuda, S
Hitomi, J
Miyata, S
Mizuno, T
Imaizumi, K
Katayama, T
Tohyama, M
机构
[1] Osaka Univ, Grad Sch Med, Dept Anat & Neurosci, Suita, Osaka 5650871, Japan
[2] Nara Inst Sci & Technol, Div Struct Cell Biol, Nara 6300101, Japan
[3] Japan Sci & Technol Corp, CREST, Kawaguchi, Saitama 3320012, Japan
关键词
IRE1; alpha; JAB1; endoplasmic reticulum; stress; unfolded protein response;
D O I
10.1016/j.neuint.2004.01.003
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Recent papers have reported that neuronal death in patients with Alzheimer's disease, Parkinson's disease, and cerebral ischemia has its origin in the endoplasmic reticulum (ER). IRE lot is one of the ER stress transducers that detect the accumulation of unfolded proteins in the ER. IRE1alpha mediates two major cellular responses, which are the unfolded protein response (UPR), a defensive response, and apoptosis that leads to cell death. However, little is known about the regulatory mechanisms that select between the UPR and apoptosis. We identified Jun activation domain-binding protein-1 (JAB1) as a molecule that interacts with IRE1alpha using a yeast two-hybrid system. We demonstrated that JAB1 binds to IRE1alpha in the absence of stress, but that binding is decreased by ER stress inducers. Moreover, mutant JAB1 down-regulates the UPR signaling pathway through tight binding with IRE1alpha. These results suggested that JAB1 may act as a key molecule in selecting the UPR or cell death by association and dissociation with IRE I (X. (C) 2004 Elsevier Ltd. All rights reserved.
引用
收藏
页码:765 / 772
页数:8
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