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Title 

FAF1 suppresses IκB kinase (IKK) activation by disrupting the IKK complex assembly

Authors 

M Y ParkJ H MoonK S LeeH I ChoiJ ChungHyo Jeong HongE Kim

Publisher 

American Society for Biochemistry and Molecular Biology

Issue Date 

2007

Citation 

Journal of Biological Chemistry, vol. 282, no. 38, pp. 27572-27577

Keywords 

amino acidsmolecular biologypolysaccharidesFas-associated factor 1 (FAF1)proinflammatory stimulistimuli convergetumor necrosis factorsFas antigenI kappa B kinaseFAF1 protein, human

Abstract 

This study presents a molecular inhibitory mechanism by Fas-associated factor 1 (FAF1) on IκB kinase (IKK) activation, where divergent NF-κB-activating stimuli converge. FAF1 interacts with IKKβ in response to proinflammatory stimuli (such as tumor necrosis factor-α, interleukin-1β, and lipopolysaccharide) and suppresses IKK activation. Interaction of the leucine-zipper domain of IKKβ with FAF1 affected the IKK heterocomplex (IKKα/β) and homocomplex (IKKα/α, IKKβ/β) formations and attenuated IKKγ recruitment to IKKβ. Overexpression of FAF1 reduced the level of IKKβ activity, whereas FAF1 depletion increased the activity. These results indicate that FAF1 inhibits IKK activation and its downstream signaling by interrupting the IKK complex assembly through physical interaction with IKKβ. Taken together, FAF1 robustly suppresses NF-κB activation through the inhibition of IKK activation in combination with previously reported cytoplasmic retention of NF-κB p65 (Park, M. Y., Jang, H. D., Lee, S. Y., Lee, K. J., and Kim, E. (2004) J. Biol. Chem. 279, 2544-2549). Such redundant suppression would prevent inadvertent activation of the NF-κB pathway.

ISSN 

0021-9258

Link 

http://dx.doi.org/10.1074/jbc.C700106200

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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