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

Biochem Soc Trans. 2023 Aug 31;51(4):1505-1520. doi: 10.1042/BST20221238.

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.

Keywords: cryo-electron microscopy; crystallography; kinesin; microtubule; molecular motors; tubulin.

Publication types

  • Review
  • Research Support, Non-U.S. Gov't
  • Research Support, N.I.H., Extramural

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Kinesins* / metabolism
  • Microtubules / metabolism
  • Myosins
  • Tubulin* / analysis
  • Tubulin* / chemistry
  • Tubulin* / metabolism

Substances

  • Kinesins
  • Tubulin
  • Adenosine Triphosphate
  • Myosins