The centrosome is a non‐membrane bound structural organelle that is crucial in spindle assembly, as the centrosomes act as the microtuble organizing centers at the spindle poles during mitosis. Deviation from normal spindle assembly can lead to activation of the spindle assembly checkpoint (SAC). Some of the most successful antimitotic drugs activate the SAC in order to arrest cancer cells in mitosis to induce subsequent apoptosis. Recently, kinesins and kinases implicated in spindle assembly have gained attention as possible therapeutic targets, as their functions rely on their ability to hydrolyze ATP. Our lab’s previous proteomic and genetic studies identified steroidogenic acute regulatory protein‐related lipid transfer domain containing 9 (STARD9) as a kinesin involved in spindle assembly. Its depletion invokes multipolar spindles in dividing cancer cells and most surprisingly, STARD9‐depleted cancer cells display increased Taxol sensitivity. STARD9 plays a functional role in the stabilization of pericentriolar material (PCM) during centriole maturation, but its mechanism of action and its regulation are not yet fully understood. To elucidate these mechanisms we have used proteomic and chemical‐genetic approaches to study both STARD9’s major domains and endogenous STARD9 protein. These approaches have identified putative interacting proteins that may play regulatory roles in PCM stabilization. We are currently focused on determining the importance of these STARD9 interactions for PCM stabilization. Our work looks to further the knowledge of STARD9’s function within centrosome assembly and more broadly cancer cell division.Support or Funding InformationUSHHS Ruth L. Kirschstein Institutional National Research Service Award #T32 CA009056