Journal
FEBS LETTERS
Volume 584, Issue 22, Pages 4672-4678Publisher
WILEY
DOI: 10.1016/j.febslet.2010.10.050
Keywords
Heat shock protein 70; Bax; c-Jun N-terminal kinase; BimL; Ultraviolet irradiation
Funding
- National Basic Research Program of China [2010CB732602]
- Program for Changjiang Scholars and Innovative Research Team in University [IRT0829]
- National Natural Science Foundation of China [30870676, 30870658]
- US National Institutes of Health (National Center for Research Resources) [P20 RR016478]
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Here we studied the mechanism by which heat shock protein 70 (Hsp70) prevents Bax activation during ultraviolet (UV)-induced apoptosis. UV treatment led to c-Jun N-terminal kinase (JNK) phosphorylation, Bim redistribution and subsequent Bax activation. Bim depletion caused a smaller reduction in apoptosis than that by JNK inhibition, indicating that Bim activation is not entirely responsible for induction of apoptosis and other mechanisms are involved. Hsp70 knockdown resulted in high levels of activated JNK and Bax, while Hsp70 overexpression inhibited these processes. These findings demonstrate that Hsp70 prevented Bax activation via inhibiting the JNK/Bim pathway. Simultaneously, increased binding of Hsp70 to Bax was observed. Collectively, our results for the first time demonstrate that Hsp70 prevents Bax activation both by inhibiting the JNK/Bim pathway and by interacting with Bax in UV-induced apoptosis. (C) 2010 Published by Elsevier B. V. on behalf of the Federation of European Biochemical Societies.
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