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J Biol Chem, Vol. 275, Issue 1, 322-327, January 7, 2000
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From the 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-xL protein. SAPK
phosphorylates Bcl-xL on threonine 47 (Thr-47) and
threonine 115 (Thr-115) in vitro and in vivo.
In contrast to wild-type Bcl-xL, a mutant
Bcl-xL 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-xL in the apoptotic response to genotoxic stress.
Division of Cancer Pharmacology, Dana-Farber
Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115, Manitoba Institute of Cell Biology, University of Manitoba,
Winnipeg, Manitoba R3EOV9, Canada, ** Oncology Research Program,
Preclinical Research, Novartis Pharmaceuticals Corp., East Hanover,
New Jersey 07936, and Department of Radiation and Cellular
Oncology, University of Chicago, Chicago, Illinois 60637
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