The mitotic spindle drives the accurate segregation of chromosomes into daughter cells during cell division. One of the multiprotein complexes that binds and stabilises spindle microtubules contains TACC3, clathrin, chTOG and GTSE1, but the exact composition and interactions between proteins of the complex remain unclear. Now, Stephen Royle and colleagues (Ryan et al., 2021) investigate these questions using the knocksideways method, which allows for acute and inducible rerouting of proteins to the mitochondria. After generating and validating cell lines endogenously tagged with FKBP–GFP, they relocalise each protein of the complex and assess what effect this has on the localisation of other member proteins, using both immunofluorescence and single-cell live imaging. Relocalising clathrin or TACC3 leads to removal of the entire complex, whereas relocalising chTOG or GTSE1 has no effect on the rest of the complex. This suggests that TACC3 and clathrin are core members, while chTOG and GTSE1 are ancillary to the TACC3–chTOG–clathrin–GTSE1 complex. The authors also clarify that the clathrin-binding protein PIK3C2A is in fact not a part of this complex, contrasting a previous report. This work has important implications for anti-mitotic cancer treatment strategies, as it shows that targeting of TACC3–clathrin interactions or their binding to microtubules is required to block the function of this complex.