To improve our understanding of the roles of microtubule cross-linking moto
rs in mitosis, we analyzed two sea urchin embryonic kinesin-related protein
s. It is striking to note that both of these proteins behave as homotetrame
rs, but one behaves as a more compact molecule than the other. These observ
ations suggest that these two presumptive motors could cross-link microtubu
les into bundles with different spacing. Both motors localize to mitotic sp
indles, and antibody microinjection experiments suggest that they have mito
tic functions. Thus, one of these kinesin-related proteins may crosslink sp
indle microtubules into loose bundles that are "tightened" by the other.