We are at an interdisciplinary lab lab, working at the interface of Biochemistry, Cell Biology and Physics. Our work is driven by a sense of curiosity, fascination and discovery.
Cellular actin dynamics are essential in key processes such as cell migration, wound healing, cell division and endocytosis. Living cells rapidly assemble and remodel their actin cytoskeleton in response to external signals to move, change their shape, and for reorganizing their internal architecture. Cells can locally tune the rates of actin dynamics depending upon the requirements of the specific biological process. But how do they do this in the complex milieu of the cytoplasm?
The central hypothesis driving our research is that intracellular actin dynamics results form an interplay between multicomponent biochemical (i.e., proteins) and mechanical factors (forces).
Our lab's research can be divided into two themes below.
Multicomponent regulation of actin dynamics
How do multiprotein ecosystems regulate actin dynamics at the two filament ends?
We employ multispectral single-molecule and high-throughput single-filament imaging to investigate how multiple proteins that bind the same site on an actin filament lead to emergent dynamics.
Mechanical regulation of actin dynamics
How do mechanical forces (e.g. tension, curvature etc.) on actin filaments influence dynamics at the two filament ends?
Actin filaments not only generate forces, but their dynamics are in turn affected by external mechanical forces. We use optical traps, magnetic tweezers and microfluidic flow-induced drag forces to investigate how the biochemical interactions of regulatory proteins with actin filaments are mediated and modulated by mechanical perturbations.
Our single molecule toolbox at the nanoscale
Total internal reflection microscopy (2 Nikon E-TIRFs + 1 iLas ring TIRF scopes)
Microfluidics (Automated flow control systems from Fluigent)
Optical tweezers (Lumicks C-Trap confocal setup)
Multispectral single molecule imaging