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J. Biol. Chem., Vol. 278, Issue 37, 35272-35278, September 12, 2003

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Heat Shock Protein 27 Association with the IB Kinase Complex Regulates Tumor Necrosis Factor -induced NF-B Activation^*

Kyu-Jin Park, Richard B. Gaynor  and Youn Tae Kwak

From the Division of Hematology-Oncology, Department of Medicine, University of Texas Southwestern Medical Center, Dallas, Texas 75390-8594

Heat shock protein 27 (Hsp27) is a ubiquitously expressed member of the heat shock protein family that has been implicated in various biological functions including the response to heat shock, oxidative stress, and cytokine treatment. Previous studies have demonstrated that heat shock proteins are involved in regulating signal transduction pathways including the NF-B pathway. In this study, we demonstrated that Hsp27 associates with the IB kinase (IKK) complex and that this interaction was stimulated by tumor necrosis factor treatment. Phosphorylation of Hsp27 by the kinase mitogen-activated protein kinase-activated protein kinase 2, a downstream substrate of the mitogen-activated protein kinase p38, enhanced the association of Hsp27 with IKK to result in decreased IKK activity. Consistent with these observations, treatment of cells with a p38 inhibitor reduced the association of Hsp27 with IKK and thus resulted in increased IKK activity. These studies indicate that Hsp27 plays a negative role in down-regulating IKK signaling by reducing its activity following tumor necrosis factor stimulation.

Received for publication, May 15, 2003 , and in revised form, June 25, 2003.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Div. of Hematology-Oncology, Dept. of Medicine, U.T. Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX 75390-8594. Tel.: 317-651-5134; Fax: 317-277-3652; E-mail: gaynor_richard{at}lilly.com.

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