Microtubule cross-linking triggers the directional motility of kinesin-5.

Published

Journal Article

Although assembly of the mitotic spindle is known to be a precisely controlled process, regulation of the key motor proteins involved remains poorly understood. In eukaryotes, homotetrameric kinesin-5 motors are required for bipolar spindle formation. Eg5, the vertebrate kinesin-5, has two modes of motion: an adenosine triphosphate (ATP)-dependent directional mode and a diffusive mode that does not require ATP hydrolysis. We use single-molecule experiments to examine how the switching between these modes is controlled. We find that Eg5 diffuses along individual microtubules without detectable directional bias at close to physiological ionic strength. Eg5's motility becomes directional when bound between two microtubules. Such activation through binding cargo, which, for Eg5, is a second microtubule, is analogous to known mechanisms for other kinesins. In the spindle, this might allow Eg5 to diffuse on single microtubules without hydrolyzing ATP until the motor is activated by binding to another microtubule. This mechanism would increase energy and filament cross-linking efficiency.

Full Text

Duke Authors

Cited Authors

  • Kapitein, LC; Kwok, BH; Weinger, JS; Schmidt, CF; Kapoor, TM; Peterman, EJG

Published Date

  • August 4, 2008

Published In

Volume / Issue

  • 182 / 3

Start / End Page

  • 421 - 428

PubMed ID

  • 18678707

Pubmed Central ID

  • 18678707

Electronic International Standard Serial Number (EISSN)

  • 1540-8140

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.200801145

Language

  • eng