Adi Paul
From WikidChem
Adi is a graduate student in the Pollard Lab.
Research
Approach: biochemical and biophysical kinetics
I'm studying formins, a class of proteins ubiquitious in eukaryotes that assemble and spatially organize linear actin structures (e.g. contractile ring during cytokinesis, stress fibers, filopodia). In vitro, formins stimulate the rate of formation of new actin filament ends (nucleation) and also influence elongation of existing filaments. Profilin, an actin-monomer binding protein, interacts with both formin and actin and thereby further influences the kinetics of both elongation (speeds up) and nucleation (slows down). As profilin-actin is the dominant form of actin in the cell, we are very interested in how polymerization proceeds in the presence of all these factors. Using microscopy and spectroscopy to observe polymerization of purified actin in the presence of recombinantly expressed profilin and formin, and computational approaches to model the numerous reactions describing polymerization and compare it to real data, I have studied the interactions between formin, profilin, and actin, to understand how these factors converge at a molecular level to influence actin polymerization in the cell.
