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J. Biol. Chem., Vol. 279, Issue 42, 43893-43899, October 15, 2004

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Integrin-linked Kinase Regulates the Nuclear Entry of the c-Jun Coactivator -NAC and Its Coactivation Potency^*

Isabelle Quélo, Claude Gauthier, Gregory E. Hannigan¶, Shoukat Dedhar||**, and René St-Arnaud

From the Genetics Unit, Shriners Hospital for Children Montréal, Québec H3G 1A6, Canada, ^¶Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, Ontario M5G 1X8, Canada, ^||British Columbia Cancer Agency and Vancouver Hospital, Jack Bell Research Center, Vancouver, British Columbia V6H 3Z6, Canada, ^**Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada, and Departments of Medicine, Surgery, and Human Genetics, McGill University, Montréal, Québec H3A 2T5, Canada

Overexpression of the integrin-linked kinase (ILK) was shown to increase c-Jun-dependent transcription. We now show that this effect of ILK involves the c-Jun transcriptional coactivator, nascent polypeptide-associated complex and coactivator (-NAC). ILK phosphorylated -NAC on residue Ser-43 upon adhesion of cells to fibronectin. Co-expression of constitutively active ILK with -NAC led to the nuclear accumulation of the coactivator. Conversely, -NAC remained in the cytoplasm of cells transfected with a dominant-negative ILK mutant, and a mutated -NAC at phosphoacceptor position Ser-43 (S43A) also localized outside of the nucleus. The S43A -NAC mutant could not potentiate the effect of ILK on c-Jun-dependent transcription. We conclude that ILK-dependent phosphorylation of -NAC induced the nuclear accumulation of the coactivator and that phosphorylation of -NAC by ILK is required for the potentiation of c-Jun-mediated responses by the kinase. The results represent one of the rare examples of a transcriptional coactivator shuttling between the cytosol and the nucleus.

Received for publication, June 7, 2004 , and in revised form, August 4, 2004.

^* This work was supported by a grant from the Shriners of North America. 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.

Present address: Aventis Pharma Deutschland GmbH, Indus-triepark Hoechst, D-65926 Frankfurt am Main, Germany.

To whom correspondence should be addressed: Genetics Unit, Shriners Hospital for Children, 1529 Cedar Ave., Montréal, Québec H3G 1A6, Canada. Tel.: 514-282-7155; Fax: 514-842-5581; E-mail: rst-arnaud{at}shriners.mcgill.ca.

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