The function of microtubules at the mitotic spindle is controlled in part by members of the kinesin-5 family. Kinesin-5 motors crosslink and slide apart antiparallel MTs and thereby facilitate the maintenance of the bipolar spindle structure and its elongation during anaphase B. In S. cerevisiae, there are two kinesin-5 homologues, Cin8 and Kip1. Cin8 destabilises the plus-ends of microtubules in early anaphase and was the first N-terminal kinesin shown to move processively to their minus-ends; it can also switch the directionality of microtubules. By contrast, much less is known with regard to the role of Kip1 in mitosis and its motile properties. Thus Larisa Gheber and co-workers (p. 4147) set out to close this knowledge gap. They find that Kip1 localises to the midzone of late-anaphase spindles (when Cin8 has already detached), which – as they show – is essential to stabilise the plus-ends of interpolar microtubules. When analysing their dynamics in detail, the authors find that interpolar microtubules depolymerise in two stages, the second of which coincides with spindle breakdown, Kip1 follows the plus-ends of interpolar microtubules and translocates towards the spindle poles. The authors also demonstrate that Kip1, similar to Cin8, is a bidirectional motor that, in vitro, under high-salt conditions, can move towards the minus-ends of microtubles. Taken together, these findings point to a unique role of Kip1 in the elongation of the anaphase spindle and its final disassembly.