Publications by authors named "Biswaprakash Mahanta"
Article Synopsis
- Formins are key proteins that promote actin filament growth by binding to the barbed ends and facilitating the addition of actin subunits through their unique FH2 and FH1 domains.
- Research on the yeast formin Bni1p showed that filament length is influenced by the elongation rate and the probability of formin dissociation, which varies under different conditions.
- The study highlights the important role of FH1 domains in controlling the processivity of formins, affecting the way filaments are assembled and their average lengths, tailored to the specific needs of the cell.
The actin cytoskeleton is a dynamic filamentous network that assembles into specialized structures to enable cells to perform essential processes. Direct visualization of fluorescently-labeled cytoskeletal proteins has provided numerous insights into the dynamic processes that govern the assembly of actin-based structures. However, accurate analysis of these experiments is often complicated by the interdependent and kinetic natures of the reactions involved.
View Article and Find Full Text PDFFormins stimulate actin polymerization by promoting both filament nucleation and elongation. Because nucleation and elongation draw upon a common pool of actin monomers, the rate at which each reaction proceeds influences the other. This interdependent mechanism determines the number of filaments assembled over the course of a polymerization reaction, as well as their equilibrium lengths.
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