The
movement of nanotube-labelled kinesin-1 motor proteins in cells was analysed
using fluorescence microscopy. At timeframes
above 100 ms, researchers observed a regime of kinesin molecular motion
different from thermal motion or directed motor activity. In this regime, the kinesins were bound to the
microtubule network, and moved randomly but remained locally constrained. Their dynamics reflected nonequilibrium fluctuations
in the microtubule network. These
fluctuations were driven by cytoplasmic myosin activity generating a random stirring
effect.
High-resolution
mapping of intracellular fluctuations using carbon nanotubes; N. Fakhri et al; Science; Vol 344(6187); p 1031
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