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Abstract

Active networks of biopolymers and motor proteins in vitro self-organize and exhibit dynamic structures on length scales much larger than the interacting individual components of which they consist. How the dynamics is related across the range of length scales is still an open question. Here, we experimentally characterize and quantify the dynamic behavior of isolated microtubule bundles that bend due to the activity of motor proteins. At the motor level, we track and describe the motion features of kinesin-1 clusters stepping within the bending bundles. We find that there is a separation of length scales by at least 1 order of magnitude. At a run length of <1 μm, kinesin-1 activity leads to a bundle curvature in the range of tens of micrometers. We propose that the distribution of microtubule polarity plays a crucial role in the bending dynamics that we observe at both the bundle and motor levels. Our results contribute to the understanding of fundamental principles of vital intracellular processes by disentangling the multiscale dynamics in out-of-equilibrium active networks composed of cytoskeletal elements.