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J. Biol. Chem., Vol. 278, Issue 26, 23561-23569, June 27, 2003

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The F-actin Cross-linking and Focal Adhesion Protein Filamin A Is a Ligand and in Vivo Substrate for Protein Kinase C^*

Ulrich Tigges , Bettina Koch , Josef Wissing , Brigitte M. Jockusch  and Wolfgang H. Ziegler  ¶

From the Department of Cell Biology, Zoological Institute and the Department of Biochemistry, Institute for Biochemistry and Biotechnology, Technical University of Braunschweig, 38092 Braunschweig, Germany

Filamin A is an established structural component of cell-matrix adhesion sites. In addition, it serves as a scaffold for the subcellular targeting of different signaling molecules. Protein kinase C (PKC) has been found associated with filamin; however, details about this interaction and its significance for cell-matrix adhesion-dependent signaling have remained elusive. We performed a yeast two-hybrid analysis using protein kinase C as a bait and identified filamin as a direct binding partner. The interaction was confirmed in transfected HeLa cells, and serial truncation fragments of filamin A were employed to identify two binding sites on filamin. In vitro ligand binding assays revealed a Ca²⁺ and phospholipid-dependent association of the regulatory domain of protein kinase C with these sites. Phosphorylation of filamin was found to be isoform-restricted, leading to phosphate incorporation in the C termini of filamin A and C, but not B. PKC-dependent phosphorylation of filamin was also detected in cells. Our data suggest an intimate interaction between filamin and PKC in cell signaling.

Received for publication, March 5, 2003 , and in revised form, April 14, 2003.

^* This work was supported by the German Research Council. 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. E-mail: w.ziegler{at}tu-bs.de.

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