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

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.

SUBMITTER: Benoit MPMH

PROVIDER: S-EPMC10586761 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature

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

Benoit Matthieu P M H MPMH Hunter Byron B Allingham John S JS Sosa Hernando H

Biochemical Society transactions 20230801 4

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 th ...[more]

PMID: 37560910

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