A5067611167- Cellular Mechanics and Interactions
- 3D Printing in Biomedical Research
- Advanced Fluorescence Microscopy Techniques
- Cell Image Analysis Techniques
- Cell Adhesion Molecules Research
- Force Microscopy Techniques and Applications
- Microtubule and mitosis dynamics
- Nuclear Structure and Function
- Cardiomyopathy and Myosin Studies
- Nanofabrication and Lithography Techniques
Emory University
2022-2025
Cells control actin assembly by regulating reactions at filament barbed ends. Formins accelerate elongation, capping protein (CP) arrests growth and twinfilin promotes depolymerization How these distinct activities get integrated within a shared cytoplasm is unclear. Using microfluidics-assisted TIRF microscopy, we find that formin, CP can simultaneously bind Three‑color, single-molecule experiments reveal cannot ends occupied formin unless present. This trimeric complex short-lived (~1 s),...
Intracellular actin networks assemble through the addition of ATP-actin subunits at growing barbed ends filaments. This is followed by "aging" filament via ATP hydrolysis and subsequent phosphate release. Aged ADP-actin thus "treadmill" before being released back into cytoplasmic monomer pool as a result depolymerization pointed ends. The necessity for aging disassembly reinforced preferential binding cofilin to aged over newly-assembled ADP-Pi in filament. Consequently, investigations how...
According to the cellular actin dynamics paradigm, filaments grow at their barbed ends and depolymerize predominantly from pointed form polar structures do productive work. We show that can elongate end when assisted by Vibrio VopF/L toxins, which act as processive polymerases. In cells, processively moving speckles are inhibited factors blocking but not ends. Multispectral single-molecule imaging confirmed VopF molecules associate with end, actively promoting its elongation even in presence...
Abstract Intracellular actin networks assemble through the addition of ATP-actin subunits at growing barbed ends filaments. This is followed by “aging” filament via ATP hydrolysis and subsequent phosphate release. Aged ADP-actin thus “treadmill” before being released back into cytoplasmic monomer pool as a result depolymerization pointed ends. The necessity for aging disassembly reinforced preferential binding cofilin to aged over newly-assembled ADP-P i in filament. Consequently,...
Living cells assemble their actin networks by regulating reactions at the barbed end of filaments. Formins accelerate elongation, capping protein (CP) arrests growth and twinfilin promotes depolymerization ends. How integrate these disparate activities within a shared cytoplasm to produce diverse networks, each with distinct morphologies finely tuned assembly kinetics, is unclear. We used microfluidics-assisted TIRF microscopy investigate how formin mDia1, CP influence elongation filament...