ABSTRACT
The Kinesin-6 family are N-terminal motor domain kinesins. Available data suggests that they are plus-end-directed translocating motors. The motor domain is followed by a region of predicted coiled-coil, followed by a C-terminal tail domain. The coiled-coil region mediates the interaction with various binding partners and is likely responsible for multimerisation. A common theme in the physiological role of the Kinesin-6 family is their involvement in cell division. Members of this family play a crucial role in regulation of cytokinesis. The activity of several Kinesin-6 family members is regulated by phosphorylation. KIF20A requires phosphorylation by PLK1 to allow completion of cytokinesis. The interaction of Klp9 and its interacting partner Ase1 is regulated via phosphorylation, with dephosphorylation of both proteins promoting their interaction and resulting in enhanced velocity of spindle elongation.
