| First Author | Tigges U | Year | 2003 |
| Journal | J Biol Chem | Volume | 278 |
| Issue | 26 | Pages | 23561-9 |
| PubMed ID | 12704190 | Mgi Jnum | J:86198 |
| Mgi Id | MGI:2678985 | Doi | 10.1074/jbc.M302302200 |
| Citation | Tigges U, et al. (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(26):23561-9 |
| abstractText | 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. |
