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Lipid diffusion enhanced by molecular motors

Gwendal Guérin, Emily Winther Sorensen, Ching‐Yun CheniD, John ManziiD, Julien BerroiD, Nikos S. HatzakisiD, Hsuan‐Yi CheniD, Feng‐Ching TsaiiD

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Abstract

An experimental study of myosin I motors on a supported lipid membrane with a nematic actin filament layer is presented. The activities of myosin I motors re-organize the actin layer, in particular the morphology of +1/2 nematic defects. Data from single-particle tracking (SPT) of lipid molecules reveal two interesting features. First, the distribution of average lipid speed over a track shows two groups of lipids (high-speed and low-speed), and the proportion of lipids to be high-speed is higher in regions rich in actin. Second, by classifying short-time movement of the lipids into normal diffusion, directed motion, confined motion, and subdiffusion states, we found that lipids in regions rich in actin have a lower probability to stay in the confined and subdiffusion states and more likely to perform normal diffusion. Furthermore, fluorescence recovery after photobleaching (FRAP) measurements show that the diffusion of lipids in the actin-rich regions is enhanced. The SPT and FRAP results suggest that myosin I motor activities turn low-speed lipids to high-speed ones, and affect the lipid moving state by reducing confined and subdiffusive motion. As a result, lipid diffusion is enhanced by motor activities.

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