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Mol. Cell. Biol. 25 (6): 2450-2462

Copyright © 2005 by the American Society for Microbiology. All rights reserved.

Sequestration of TRAF2 into Stress Granules Interrupts Tumor Necrosis Factor Signaling under Stress Conditions

Woo Jae Kim,1,{dagger} Sung Hoon Back,1,{dagger} Vit Kim,1 Incheol Ryu,1, and Sung Key Jang1*

National Research Laboratory, Postech Biotech Center, Department of Life Science, Division of Molecular and Life Sciences, Pohang University of Science and Technology, Pohang, Kyungbuk, Korea1

Received for publication 26 August 2004. Revision received 14 September 2004. Accepted for publication 24 November 2004.

Abstract: The cellular stress response (SR) is a phylogenetically conserved protection mechanism that involves inhibition of protein synthesis through recruitment of translation factors such as eIF4G into insoluble stress granules (SGs) and blockade of proinflammatory responses by interruption of the signaling pathway from tumor necrosis factor alpha (TNF-{alpha}) to nuclear factor-{kappa}B (NF-{kappa}B) activation. However, the link between these two physiological phenomena has not been clearly elucidated. Here we report that eIF4GI, which is a scaffold protein interacting with many translation factors, interacts with TRAF2, a signaling molecule that plays a key role in activation of NF-{kappa}B through TNF-{alpha}. These two proteins colocalize in SGs during cellular exposure to stress conditions. Moreover, TRAF2 is absent from TNFR1 complexes under stress conditions even after TNF-{alpha} treatment. This suggests that stressed cells lower their biological activities by sequestration of translation factors and TRAF2 into SGs through a protein-protein interaction.

* Corresponding author. Mailing address: NRL, PBC, Department of Life Science, Division of Molecular and Life Sciences, Pohang University of Science and Technology, Hyoja-Dong San 31, Pohang, Kyungbuk 790-784, Korea. Phone: 82 54 279 2298. Fax: 82 54 279 8009. E-mail: sungkey{at}postech.ac.kr.

{dagger} W.J.K. and S.H.B. contributed equally to the work.

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