title: Review: regulation mechanisms of Kinesin-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.
authors.affiliation: Institute for Cell Biology, University of Munich, Schillerstr. 42, D-80336, Munich, Germany.
authors.forename: Sarah
authors.initials: S
authors.lastname: Adio
authors.forename: Jolante
authors.initials: J
authors.lastname: Reth
authors.forename: Friederike
authors.initials: F
authors.lastname: Bathe
authors.forename: Günther
authors.initials: G
authors.lastname: Woehlke
mesh_terms: D000818:Animals; D002465:Cell Movement / Q000502:physiology*; D005658:Fungi / Q000378:metabolism; D006801:Humans; D016547:Kinesins / Q000378:metabolism*; D008870:Microtubules / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology*
chemical_list: D016547:Kinesins