In cells, the assembly of actin filaments is highly regulated to give rise to various actin networks of well-controlled architectures such as the cortex, lamellipodia, filopodia, ... This results in specific deformations and movements that are required for many processes (cell motility, cell division, endocytosis, vesicle transport…).
Actin-binding proteins are key regulators controlling how, where and when actin monomers will assemble into filaments. Understanding their biochemical regulatory activities can be very challenging, especially when multiple activities coexist within a single protein or a stable complex, and is also highly dependent on the local cellular environment.
Mechanics play a central role, as the actin cytoskeleton generates and transmits mechanical forces throughout cells and tissues. Growing evidence shows that the cytoskeleton senses mechanical forces, and is directly involved in the conversion of mechanical information into chemical signals. Yet very little is known about the elementary processes of actin mechano-sensitivity. Our goal is to understand how mechanical constraints affect actin dynamics and the action of regulatory proteins.
Our lab has developed biophysical experimental approaches based on microfluidics and micropatterning in order to address these questions and unveil the elementary mechanical and chemical processes regulating actin assembly. We believe that single filament experiments, in addition to standard biochemical assays, are essential and keys to decipher the individual molecular reactions regulating the emergence of actin networks.
Here, you can find an overview of our research about actin dynamics regulation and our publications.
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