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The unique approach undertaken in our laboratory to study mitotic dynamics relies on combining in vivo and in vitro assays to study the function and regulation of bi-directional kinesin motor proteins. Since mitotic molecular motor proteins perform their intracellular function by binding and moving along MTs, this approach enables us to understand both the molecular mechanisms that enable bi-directional motility and the physiological importance of such motility. The methodology that we apply includes both in vitro assays (namely, single-molecule fluorescence motility, multi-motor MT gliding, and antiparallel MT-sliding) and in vivo assays (namely, localization to the spindle of GFP-tagged kinesin motor variants and mutants, spindle and MT dynamics in cells expressing tubulin-GFP, viability of cells deleted for the chromosomal copies of the kinesin motors and expressing mutants of these motors for plasmids, cell-cycle analysis, and phosphorylation analysis of the proteins in question.