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Papers In Press, published online ahead of print January 29, 2001
J. Biol. Chem, 10.1074/jbc.M010677200
Submitted on November 27, 2000
Revised on January 26, 2001
Accepted on January 29, 2001

Activation of Caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2 (TRAF2) dependent mechanism in response to the ER stress

Takunari Yoneda, Kazunori Imaizumi, Kayoko Oono, Daishi Yui, Fumi Gomi, Taiichi Katayama, and Masaya Tohyama

Anatomy and Neuroscience, A-2, Osaka University Medical School, Suita, Osaka 565-0871

Corresponding Author: yoneda{at}anat2.med.osaka-u.ac.jp

When accumulation of malfolded protein in the endoplastic reticulum (ER) is induced by various adverse conditions, such as hypoxia, glucose starvation and perturbation of calcium homeostasis, cells respond to the stress by increasing transcription of genes encoding ER molecular chaperones (unfolded protein response, UPR). The signaling is initiated by IRE1s, ER stress sensors. Alternatively, excessive stress to the ER results in apoptosis. Caspase-12 is known to be essential for this ER stress induced apoptosis. In this study, we analyzed the detailed regulatory mechanisms of IRE1s during ER stress. We identified JIK as a binding partner of IRE1a and JIK was seen to modulate IRE1a-TRAF2 complex formation and the resultant alteration to JNK signaling from IRE1s in response to ER stress. We also demonstrated that TRAF2 interacts with procaspase-12 and promotes clustering of procaspase-12 and its activation by cleavage in response to ER stress. These results indicate that TRAF2 plays crucial roles not only in the signaling of the JNK pathway but also in activation of caspase-12 to transduce signals from IRE1s. Thus, we provide a missing link in the ER stress induced apoptosis signaling pathway, one which connects the stress sensor molecule IRE1s and the activation of caspase-12.


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