We report an experimental study of the kinetics of actin assembly mediated by branching and capping proteins. Our findings confirm the recent prediction of a "branching explosion" occurring during polymerization. Fluorescence imaging shows a number of actin filaments with branches within a few minutes of polymerization, induced by the activated branching protein complex Arp2/3, but the number of visible branches decreases over time. The light-scattering intensity displays an overshoot as a function of time, which we attribute to the formation of highly branched clusters early in polymerization. Furthermore, the overshoot occurs over a limited range of the ratio of concentrations of branching and capping proteins, also consistent with the theoretical model. These results establish a natural link between the kinetic theory of actin assembly in vitro and the cytoskeletal structure and actin dynamics in motile cells.
|Journal||Physical Review E - Statistical, Nonlinear, and Soft Matter Physics|
|State||Published - Oct 9 2009|