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K1/MEKK4 are responsible for TRAIL-induced JNK/p38 phosphorylation

Authors
 Bo K Sun ; Joo-Hang Kim ; Jae J. Song ; Yong J. Lee ; Hye J. Choi ; Hye J. ; So Y. Kim ; Seeun Oh ; Hoan N. Nguyen 
Citation
 Oncology Reports, Vol.25(2) : 537~544, 2011 
Journal Title
 Oncology Reports 
ISSN
 1021-335X 
Issue Date
2011
Abstract
The tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) has been shown to activate mitogen-activated protein kinases (MAPKs) depending on caspase and mammalian sterile 20-like kinase 1 activations. However, the upstream molecule of MAPKs has not yet been identified. The mitogen-activated protein kinase kinase 1 (MEKK1) and the apoptosis signal-regulating kinase 1 (ASK1) are considered to be possible candidates for the action of MAPKKKs induced by TRAIL and the possibility of reactive oxygen species involvement has also been investigated. We found that MEKK1/MEKK4 as opposed to ASK1, are responsible for TRAIL-induced c-Jun NH2-terminal kinase (JNK) or p38 activation, and that their catalytic activity is repressed by the caspase-8 inhibitor, suggesting that the caspase-8 activation induced by TRAIL is indispensible for MEKK activation. The 14-3-3 θ was also shown to interact with and to dissociate from MEKK1 by TRAIL treatment, thus implicating the 14-3-3 protein as a negative regulator of MEKK1 activation. Taken together, we show herein that the upstream molecule of the TRAIL-induced MAPK activation is MEKK, as opposed to ASK1, via the mediation of its signal through JNK/p38 in a caspase-8-dependent manner.
URI
http://ir.ymlib.yonsei.ac.kr/handle/22282913/92574
DOI
10.3892/or.2010.1079
Appears in Collections:
1. 연구논문 > 1. College of Medicine > Yonsei Biomedical Research Center
1. 연구논문 > 1. College of Medicine > Dept. of Internal Medicine
1. 연구논문 > 1. College of Medicine > Medical Research Center
1. 연구논문 > 5. Research Institutes > Institute for Cancer Research
Yonsei Authors
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