The T. brucei homolog of polo-like kinase (TbPLK) is an essential regulator of cell morphogenesis. We performed proteomic screens to identify potential TbPLK interactors to better understand the molecular mechanisms of kinase function. We found a cohort of uncharacterized proteins that are essential components of morphogenic cytoskeletal organelles. Domain analysis and depletion experiments on cohort members have identified their functions and mode of TbPLK interaction. This work provides the foundation for establishing the molecular networks through which TbPLK directs cell division in T. brucei.