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J. Biol. Chem., Vol. 283, Issue 15, 10089-10096, April 11, 2008

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Cell Adhesion-dependent Cofilin Serine 3 Phosphorylation by the Integrin-linked Kinase·c-Src Complex^*

Yong-Bae Kim, Suyong Choi, Moon-Chang Choi, Min-A Oh, Sin-Ae Lee, Moonjae Cho^¶, Kensaku Mizuno^||, Sung-Hoon Kim^**1, and Jung Weon Lee²

From the Departments of Tumor Biology and Molecular & Clinical Oncology, Cancer Research Institute, Cell Dynamics Research Center, College of Medicine, Seoul National University, Seoul 110-799, Korea, the ^¶Department of Medicine, Cheju National University, Jeju 690-756, Korea, the ^||Department of Biomolecular Sciences, Graduate School of Life Sciences, Tohoku University, Sendai 980-8578, Japan, and the ^**College of Oriental Medicine, Kyunghee University, Seoul 131-701, Korea

Integrin-linked kinase (ILK) is involved in signal transduction by integrin-mediated cell adhesion that leads to dynamic actin reorganization. Actin (de)polymerization is regulated by cofilin, the Ser³ phosphorylation (pS³cofilin) of which inhibits its actin-severing activity. To determine how ILK regulates pS³cofilin, we examined the effects of ILK on pS³cofilin using normal RIE1 cells. Compared with suspended cells, fibronectin-adherent cells showed enhanced pS³cofilin, depending on ILK expression and c-Src activity. The ILK-mediated pS³cofilin in RIE1 cells did not involve Rho-associated kinase, LIM kinase, or testicular protein kinases, which are known to be upstream of cofilin. The kinase domain of ILK, including proline-rich regions, appeared to interact physically with the Src homology 3 domain of c-Src. In vitro kinase assay revealed that ILK immunoprecipitates phosphorylated the recombinant glutathione S-transferase-cofilin, which was abolished by c-Src inhibition. Interestingly, epidermal growth factor treatment abolished the ILK effects, indicating that the linkage from ILK to cofilin is biologically responsive to extracellular cues. Altogether, this study provides evidence for a new signaling connection from ILK to cofilin for dynamic actin polymerization during cell adhesion, depending on the activity of ILK-associated c-Src.

Received for publication, October 5, 2007 , and in revised form, February 1, 2008.

^* This work was supported by the Korea Science and Engineering Foundation Grant from the Korean Government (Ministry of Science and Technology) (Grant R13-2007-019-00000-0 to S.-H. K. and Cell Dynamics Research Center Grant R11-2007-007-01004-0 to J. W. L.). 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.

¹ To whom correspondence may be addressed. Tel.: 82-31-201-2179; Fax: 82-31-205-1074; E-mail: sungkim7{at}khu.ac.kr.

² To whom correspondence may be addressed: Cancer Research Inst., College of Medicine, Seoul National University, Seoul 110-799, Korea. Tel.: 82-2-3668-7030; Fax: 82-2-766-4487; E-mail: jwl{at}snu.ac.kr.

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