【正文】
model, in which kinesin5 and opposing motor proteins act between overlapping microtubules2, 4, 5. However, the precise roles of kinesin5 during this process are unknown. Here we show that the vertebrate kinesin5 Eg5 drives the sliding of microtubules depending on their relative orientation. We found in controlled in vitro assays that Eg5 has the remarkable capability of simultaneously moving at 20 nm s1 towards the plusends of each of the two microtubules it crosslinks. For antiparallel microtubules, this results in relative sliding at 40 nm s1, parable to spindle pole separation rates in vivo6. Furthermore, we fo