| Autor: |
Kharbanda, S, Saxena, S, Yoshida, K, Pandey, P, Kaneki, M, Wang, Q, Cheng, K, Chen, Y N, Campbell, A, Sudha, T, Yuan, Z M, Narula, J, Weichselbaum, R, Nalin, C, Kufe, D |
| Zdroj: |
Journal of Biological Chemistry; January 2000, Vol. 275 Issue: 1 p322-7, 6p |
| Abstrakt: |
Activation of the stress-activated protein kinase (SAPK/JNK) by genotoxic agents is necessary for induction of apoptosis. We report here that ionizing radiation ionizing radiation exposure induces translocation of SAPK to mitochondria and association of SAPK with the anti-apoptotic Bcl-x(L) protein. SAPK phosphorylates Bcl-x(L) on threonine 47 (Thr-47) and threonine 115 (Thr-115) in vitro and in vivo. In contrast to wild-type Bcl-x(L), a mutant Bcl-x(L) with the two threonines substituted by alanines (Ala-47, Ala-115) is a more potent inhibitor of ionizing radiation-induced apoptosis. These findings indicate that translocation of SAPK to mitochondria is functionally important for interactions with Bcl-x(L) in the apoptotic response to genotoxic stress. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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