Research Focus

At the base of actin cytoskeleton networks formation lies a universal scheme : the assembly of ATP-actin monomers into filaments. This process involves ATP hydrolysis that leads to a major change of the actin conformation, thus of the actin filament itself.



In cells, actin assembly is regulated by hundreds of Actin Binding Proteins (ABPs), that may act together synergistically or antagonistically. 


They can bind to filament sides, filament ends, and/or monomers and have a variety of effects. We typically distinguish nucleators, proteins that modulates elongations (favoring or blocking it), and proteins that promotes filament disassembly.  Higher order structure can be obtained by proteins that link filaments between them, creating bundles or fibers.



To understand how all these ABPs generates networks of various geometries, dynamics and life-spans, our team focuses its effort to observe and manipulate single actin filaments in vitro.