Upon ligand binding, epidermal growth factor receptor (EGFR) either undergoes degradation within lysosomes, or is recycled back to the membrane for further signalling. The former leads to cessation of signalling, whereas the latter enhances cell proliferation and migration, which are cancer hallmarks. Receptor signalling and downstream cell fates are thus intimately linked to the localisation of receptor-containing endosomes within cells, but the role of motor proteins in controlling this signalling has been unstudied due to the lack of techniques to visualize motor activity in live cells. Recently, we found that transient interactions between motor proteins and endosomes regulate receptor sorting (Tirumala,Redpath et al., JCB 2024). Crucially, how often a motor protein interacted with a receptor-containing endosome was in proportion to number of adaptor proteins on the endosome. Thus, we hypothesised that receptor movement is regulated by the early recruitment of adaptor proteins to achieve different sorting outcomes. Using a combination of single-molecule, live-cell imaging, optogenetics, CRISPR cell models, endosomal pulldowns coupled with proteomics, and mathematical modelling of motor-driven endosomal transport, we are in the process of mapping out how motor adaptors regulate receptor movement and function. Ultimately, we will employ the lessons learned in this work to manipulate cargo localisation and signalling in a motor-adaptor protein-driven fashion, and therefore alter cell fates.