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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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Free article

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

S Kharbanda et al. J Biol Chem. .
Free article

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. 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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