The Diaphanous-related formin dDia2 is required for the formation and maintenance of filopodia

• Published in: Nature cell biology Vol. 7; no. 6; pp. 619 - 625
• Main Authors: Faix, Jan, Schirenbeck, Antje, Bretschneider, Till, Arasada, Rajesh, Schleicher, Michael
• Format: Journal Article
• Language: English
• Published: England Nature Publishing Group 01.06.2005
• Subjects: Actin; Actin Cytoskeleton - metabolism; Actin Cytoskeleton - ultrastructure; Animals; Carrier Proteins - genetics; Carrier Proteins - metabolism; Cell migration; Cell Movement - physiology; Control; Cytokinesis; Dictyostelium - cytology; Dictyostelium - metabolism; Dictyostelium discoideum; Drosophila Proteins - genetics; Drosophila Proteins - metabolism; Fetal Proteins; Green Fluorescent Proteins - genetics; Microfilament Proteins - genetics; Microfilament Proteins - isolation & purification; Microfilament Proteins - metabolism; Nuclear Proteins; Physiological aspects; Protozoan Proteins - genetics; Protozoan Proteins - isolation & purification; Protozoan Proteins - metabolism; Pseudopodia - metabolism; Pseudopodia - ultrastructure; Recombinant Fusion Proteins - genetics; Recombinant Fusion Proteins - metabolism; Germany
• ISSN: 1465-7392; 1476-4679; 1476-4679
• DOI: 10.1038/ncb1266

Formins have important roles in the nucleation of actin and the formation of linear actin filaments, but their role in filopodium formation has remained elusive. Dictyostelium discoideum Diaphanous-related formin dDia2 is enriched at the tips of filopodia and interacts with profilin II and Rac1. An FH1FH2 fragment of dDia2 nucleated actin polymerization and removed capping protein from capped filament ends. Genetic studies showed that dDia2 is important for cell migration as well as the formation, elongation and maintenance of filopodia. Here we provide evidence that dDia2 specifically controls filopodial dynamics by regulating actin turnover at the barbed ends of actin filaments.