Review: regulation mechanisms of Kinesin-1

  • SARAH ADIO
  • JOLANTE RETH
  • FRIEDERIKE BATHE
  • GÜNTHER WOEHLKE
Article

DOI: 10.1007/s10974-005-9054-1

Cite this article as:
ADIO, S., RETH, J., BATHE, F. et al. J Muscle Res Cell Motil (2006) 27: 153. doi:10.1007/s10974-005-9054-1

Abstract

Kinesin-1 microtubule motors are common kinesin motors from protozoa, fungi and animals. They transport vesicular or particle cargo in a strictly regulated manner. The relatively well-studied tail inhibition mechanism is based on a conformational change that leads to an interaction of Kinesin-1’s tail with the junction of neck and hinge regions. This folding causes a decrease in microtubule binding and motor activity. In fungal Kinesin-1 motors several lines of evidence suggest that a conserved tyrosine in the neck coiled-coil mediates this inhibition. In the active state, a region surrounding a conserved tryptophan in the hinge stabilises the neck coiled-coil, and prevents the tyrosine from inhibiting. Although animal and fungal Kinesin-1 motors are clearly homologous and function according to the same chemo-mechanical mechanism, they differ in their regulation. Unlike fungal Kinesin-1s, animal kinesins associate with light chains that are important for regulation and cargo interaction. Several proteins interacting with animal Kinesin-1 heavy or light chains are known, among them typical scaffolding proteins that seem to link Kinesin-1 to signalling pathways.

Copyright information

© Springer Science+Business Media, Inc. 2006

Authors and Affiliations

  • SARAH ADIO
    • 1
  • JOLANTE RETH
    • 1
  • FRIEDERIKE BATHE
    • 1
  • GÜNTHER WOEHLKE
    • 1
  1. 1.Institute for Cell BiologyUniversity of MunichMunichGermany