Regensburg 2007 – scientific programme

Parts | Days | Selection | Search | Downloads | Help

BP: Fachverband Biologische Physik

BP 16: Poster Session I

BP 16.29: Poster

Tuesday, March 27, 2007, 17:00–19:30, Poster D

Force generation in a filopodia model system — •Simone Köhler¹, Mireille Claessens¹, Michael Schleicher², and Andreas Bausch¹ — ¹TUM Physik Department E22, James Franck Straße, D-85747 Garching — ²LMU Institute for Cell Biology, Schillerstraße, D-80336 München

Formins are multi-domain proteins with a highly conserved formin-homology domain 2, that can nucleate actin filaments from monomers alone and may even trigger filament growth by a processive capping mechanism. A formin of the slime mould Dictyostelium discoideum, dDia2, has been shown to be important for the formation, elongation and maintenance of filopodia. Fascin, an actin-bundling protein is essential for filopodial protrusion, too. For further understanding the interaction of these two proteins in vitro experiments have to be done.

We study the role of fascin on assembly rates and force generation by dDia2-induced actin polymerisation using total internal reflection fluorescence microscopy (TIRFM) as well as an in vitro motility assay. In the motility assay the force generated by actin polymerisation can be used to propell formin coated beads in a medium containing only purified proteins while TIRFM allows to follow the polymerisation of single actin filaments from dDia2 immobilized on a surface.