Abstract
Cytoplasmic dynein is essential for intracellular transport. Despite extensive in vitro characterizations, how the dynein motors work collectively to transport vesicles and how they step in live cells remains elusive because of the much faster speed of dynein under physiological conditions. To dissect the molecular mechanism and dynamics of dynein, we developed novel optical probes which enabled long-term single particle tracking with high spatiotemporal resolutions. We found that the number of active dynein motors transporting the cargo switched stochastically from one to five pairs during the long-range transport. Our very bright optical probes allowed the observation of individual molecular steps. The dwell time between steps was found to be described by two equal and temperature-dependent rate constants. This finding suggests that two ATP molecules were hydrolyzed sequentially during each dynein step. Our observations shed new light on the chemomechanical cycle of dynein in living cells.
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