ABSTRACT
The Kinesin-13 family is a group of specialist microtubule-depolymerising motors. Members of this family studied to date function as homodimers. The motor domain is located centrally in the primary sequence and is flanked by divergent N- and C-terminal regions, which are responsible for cellular localisation, regulation and dimerisation. A short, typically positively charged region, called the neck, lies N-terminal to the motor domain. The Kinesin-13 family are a group of microtubule-depolymerising kinesins and members of this family are suggested to be major regulators of microtubule length. The most highly studied Kinesin-13, MCAK, has no translocating activity but displays diffusive movement on the microtubule lattice with no directional bias. Kinesin-13s likely drive microtubule depolymerisation by stabilising a curved conformation of tubulin that destabilises the microtubule. Kinesin-13s have been shown to stabilise microtubule protofilament curls and rings in the presence of a non-hydrolysable ATP analogue.
