The structural kinetics of switch-1 and the neck linker explain the functions of kinesin-1 and Eg5
- Author(s): Muretta, JM
- Jun, Y
- Gross, SP
- Major, J
- Thomas, DD
- Rosenfeld, SS
- et al.
Published Web Locationhttps://doi.org/10.1073/pnas.1512305112
Kinesins perform mechanical work to power a variety of cellular functions, from mitosis to organelle transport. Distinct functions shape distinct enzymologies, and this is illustrated by comparing kinesin-1, a highly processive transport motor that can work alone, to Eg5, a minimally processive mitotic motor that works in large ensembles. Although crystallographic models for both motors reveal similar structures for the domains involved in mechanochemical transductionâ€"including switch-1 and the neck linkerâ€"how movement of these two domains is coordinated through the ATPase cycle remains unknown. We have addressed this issue by using a novel combination of transient kinetics and time-resolved fluorescence, which we refer to as â€œstructural kinetics,â€to map the timing of structural changes in the switch-1 loop and neck linker. We find that differences between the structural kinetics of Eg5 and kinesin-1 yield insights into how these two motors adapt their enzymologies for their distinct functions.
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