Review: regulation mechanisms of Kinesin-1

J Muscle Res Cell Motil. 2006;27(2):153-60. doi: 10.1007/s10974-005-9054-1. Epub 2006 Feb 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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Cell Movement / physiology*
  • Fungi / metabolism
  • Humans
  • Kinesin / metabolism*
  • Microtubules / metabolism*
  • Signal Transduction / physiology*

Substances

  • Kinesin