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J. Biol. Chem., Vol. 280, Issue 18, 18108-18119, May 6, 2005

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HSP25 Inhibits Protein Kinase C-mediated Cell Death through Direct Interaction^*

Yoon-Jin Lee, Dae-Hoon Lee, Chul-Koo Cho, Sangwoo Bae, Gil-Ja Jhon¶, Su-Jae Lee||, Jae-Won Soh**, and Yun-Sil Lee

From the Laboratory of Radiation Effect and ^||Laboratory of Experimental Radiation Therapeutics, Korea Institute of Radiological and Medical Sciences, Seoul 139-706, ^¶Division of Molecular Life Science, Ewha Woman's University, Seoul 120-750, and ^**Laboratory of Signal Transduction, Department of Chemistry, Inha University, Incheon, 402-751 Seoul, Korea

Heat shock protein 25 (HSP25) interferes negatively with apoptosis through several pathways that involve its direct interaction with cytochrome c or Akt. Here we show that HSP25 inhibits protein kinase C (PKC) -mediated cell death through direct interaction. HSP25 binds to kinase-active PKC to inhibit its kinase activity and translocation to the membrane, which results in reduced cell death. Deletion constructs of HSP25 and PKC identified amino acids 90-103 of HSP25 and the C-terminal V5 region of PKC as binding sites. In addition, the interaction between HSP25 and PKC induced HSP25 phosphorylation at Ser-15 and Ser-86, and these phosphorylations permitted HSP25 release from PKC. Based on these observations, we propose that after PKC activation, HSP25 binds to the exposed V5 region of PKC. This novel function of HSP25 accounts for its cytoprotective properties via the inhibition of PKC and the enhancement of HSP25 phosphorylation.

Received for publication, January 31, 2005 , and in revised form, February 23, 2005.

^* This work was supported by the Korean Institute of Science and Technology Evaluation and Planning and by the Ministry of Science and Technology through the National Nuclear Technology Program. 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.

Both authors contributed equally to this work.

To whom correspondence should be addressed: Laboratory of Radiation Effect, Korea Institute of Radiological and Medical Sciences, 215-4 Gongneung-Dong, Nowon-Ku, Seoul 139-706, Korea. Tel.: 82-2-970-1325; Fax: 82-2-970-2402; E-mail: yslee{at}kcch.re.kr.

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