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Updated: Jul 19, 2025

Assembling Molecular Shuttles Powered by Reversibly Attached Kinesins
Published on: January 26, 2019
New insights into the mechanochemical coupling mechanism of kinesin-microtubule complexes from their high-resolution
Matthieu P M H Benoit1, Byron Hunter2, John S Allingham2
1Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, U.S.A.
Abstract:
Kinesin motor proteins couple mechanical movements in their motor domain to the binding and hydrolysis of ATP in their nucleotide-binding pocket. Forces produced through this 'mechanochemical' coupling are typically used to mobilize kinesin-mediated transport of cargos along microtubules or microtubule cytoskeleton remodeling. This review discusses the recent high-resolution structures (<4 Å) of kinesins bound to microtubules or tubulin complexes that have resolved outstanding questions about the basis of mechanochemical coupling, and how family-specific modifications of the motor domain can enable its use for motility and/or microtubule depolymerization.
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