Research Projects

Cell migration is critical for various physiological and pathological events, including embryonic morphogenesis, wound healing, immunological surveillance, and cancer cell invasion. Actin cytoskeleton plays a crucial role in cell migration by providing structural support for cellular protrusions like lamellipodia, invadopodia, and filopodia. Remodeling of the actin cytoskeleton, involving both assembly and disassembly of actin filaments, is essential for achieving spatial organization required for cellular motility. Formins, a group of actin binding proteins, play a vital role in regulating the cytoskeleton's assembly and disassembly. Around 15 different types of formins exist in humans, each with specific cellular localizations and functions. The activity of formins is strictly controlled by formin-binding proteins (FBP), which interact with the poly-proline-rich FH1 domain of formins. FBPs can also influence the cellular localization and activity of formins. Our recent research has revealed crucial insights into the binding interaction between the FH1 domain of FMN1 and the WW1 domain of FNBP4. FMN1 contributes to cell motility by aiding in the protrusion of the cell's leading edge and formation of focal adhesions. FNBP4 plays a role in promoting the proliferation and metastasis of hepatocellular carcinoma cells. However, further research is needed to fully understand the mechanisms by which FNBP4 promotes disease progression. The proposed study aims to investigate the role of FNBP4 in promoting cancer cell migration by examining its effects on regulating formin1 and the actin cytoskeleton. To achieve this, the study will use in vitro reconstitution assays of actin cytoskeleton dynamics and support cell biological experiments to explore the potential of FNBP4 as a cytoskeleton regulator with the following key objectives: (i) Role of FNBP4 in Formin1 regulations, (ii) Role of FNBP4 in actin cytoskeleton regulation, (iii) Investigating FNBP4 function in cell migration. The successful accomplishment of the objectives outlined in this proposal would enhance our comprehension of the regulatory mechanisms of FMN1 through FNBP4, as a novel actin binding protein. The study of these proteins could provide valuable insight into how they specifically regulate the actin cytoskeleton during cell migration. The broader implications of this research are significant. By deepening our understanding of the mechanisms that govern the cytoskeleton's proper functioning, we may be able to develop new strategies to prevent or treat diseases that result from cytoskeletal dysfunction.