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. 2000 Jan 7;275(1):322-7.
doi: 10.1074/jbc.275.1.322.

Translocation of SAPK/JNK to mitochondria and interaction with Bcl-x(L) in response to DNA damage

S Kharbanda  1 , S Saxena, K Yoshida, P Pandey, M Kaneki, Q Wang, K Cheng, Y N Chen, A Campbell, T Sudha, Z M Yuan, J Narula, R Weichselbaum, C Nalin, D Kufe
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"V体育官网" Translocation of SAPK/JNK to mitochondria and interaction with Bcl-x(L) in response to DNA damage

S Kharbanda et al. J Biol Chem. .
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"V体育官网" Erratum in

  • J Biol Chem 2000 Jun 23;275(25):19433

Abstract

Activation of the stress-activated protein kinase (SAPK/JNK) by genotoxic agents is necessary for induction of apoptosis VSports手机版. 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. .

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