PMID:12704190

Citation	Tigges, U, Koch, B, Wissing, J, Jockusch, BM and Ziegler, WH (2003) The F-actin cross-linking and focal adhesion protein filamin A is a ligand and in vivo substrate for protein kinase C alpha. J. Biol. Chem. 278:23561-9
Abstract	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 Calpha 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.
Links	PubMed Online version:10.1074/jbc.M302302200
Keywords	Actins/metabolism; Binding Sites; Calcium; Contractile Proteins/metabolism; Focal Adhesions/chemistry; Humans; Ligands; Microfilament Proteins/metabolism; Phospholipids; Phosphorylation; Protein Binding; Protein Isoforms/metabolism; Protein Kinase C/metabolism; Protein Kinase C-alpha; Signal Transduction; Two-Hybrid System Techniques
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