New insights into the mechanochemical coupling mechanism of kinesin-microtubule complexes from their high-resolution structures

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 & ANGS;) 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.

Automated summary

This review discusses recent high-resolution structures of kinesins bound to microtubules or tubulin complexes, which have resolved outstanding questions about the basis of mechanochemical coupling and how modifications of the motor domain enable motility and/or microtubule depolymerization.