Kinesin-3 motors are fine-tuned at the molecular level to endow distinct mechanical outputs

Autor: Pushpanjali Soppina, Nishaben Patel, Dipeshwari J. Shewale, Ashim Rai, Sivaraj Sivaramakrishnan, Pradeep K. Naik, Virupakshi Soppina
Jazyk: angličtina
Rok vydání: 2022
Předmět:
Zdroj: BMC Biology, Vol 20, Iss 1, Pp 1-23 (2022)
Druh dokumentu: article
ISSN: 1741-7007
DOI: 10.1186/s12915-022-01370-8
Popis: Abstract Background Kinesin-3 family motors drive diverse cellular processes and have significant clinical importance. The ATPase cycle is integral to the processive motility of kinesin motors to drive long-distance intracellular transport. Our previous work has demonstrated that kinesin-3 motors are fast and superprocessive with high microtubule affinity. However, chemomechanics of these motors remain poorly understood. Results We purified kinesin-3 motors using the Sf9-baculovirus expression system and demonstrated that their motility properties are on par with the motors expressed in mammalian cells. Using biochemical analysis, we show for the first time that kinesin-3 motors exhibited high ATP turnover rates, which is 1.3- to threefold higher compared to the well-studied kinesin-1 motor. Remarkably, these ATPase rates correlate to their stepping rate, suggesting a tight coupling between chemical and mechanical cycles. Intriguingly, kinesin-3 velocities (KIF1A > KIF13A > KIF13B > KIF16B) show an inverse correlation with their microtubule-binding affinities (KIF1A
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