Cleavage of the membrane-bound transcription factor OASIS in response to endoplasmic reticulum stress

被引:123
作者
Murakami, T
Kondo, S
Ogata, M
Kanemoto, S
Saito, A
Wanaka, A
Imaizumi, K
机构
[1] Miyazaki Univ, Div Mol & Cellular Biol, Dept Anat, Fac Med, Kiyotake, Miyazaki 8891692, Japan
[2] Nara Inst Sci & Technol, Div Struct Cellular Biol, Nara, Japan
[3] Nara Med Univ, Dept Anat, Kashihara, Nara 634, Japan
关键词
endoplasmic reticulum stress; old astrocyte specifically induced substance; regulated intramembrane proteolysis; transcription factor; unfolded protein response;
D O I
10.1111/j.1471-4159.2005.03596.x
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
When unfolded or misfolded proteins accumulate in the endoplasmic reticulum (ER), unfolded protein response (UPR) signals are transmitted from the ER to the nucleus and cytoplasm to facilitate protein folding. OASIS (old astrocyte specifically induced substance) is an ER stress transducer in astrocytes, a membrane-bound transcription factor that activates genes in the ER stress response. When unfolded proteins accumulate in the ER, OASIS is cleaved at the membrane to release its cytoplasmic domain, which then enters the nucleus and activates target genes. Here, we showed that OASIS is processed by Site-1 and -2 proteases (S1P and S2P), enzymes that reside at the Golgi apparatus and process activating transcription factor 6 (ATF6) in response to ER stress. We also showed that the cleavage of OASIS is triggered by its translocation to the Golgi apparatus. All deletion mutants for luminal domain of OASIS showed that proteolytic processing and translocation to the Golgi apparatus remained intact, indicating that OASIS does not have significant sequences for Golgi localization signals, different from the case of ATF6, and that there could be other systems for translocation of OASIS to the Golgi apparatus in response to ER stress.
引用
收藏
页码:1090 / 1100
页数:11
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