The Golgi complex is a crucial site for intracellular trafficking within eukaryotic cells. Efficient transport of cargo from the Golgi requires actin-dependent myosin motors. Although several myosins regulating this step had previously been identified, Kristine Schauer and co-workers (Capmany et al, 2019) have now carried out a systematic screen to identify further motor proteins important for Golgi function. Through siRNA depletion of 36 different myosins, combined with automated detection of changes in Golgi morphology, the authors discover MYO1C as a novel protein required for trafficking across the Golgi. They find evidence that MYO1C depletion caused decompaction and fragmentation of the Golgi complex similar to the effects of depletion of MYO18A, a previously known Golgi myosin. Their analysis further shows that MYO1C localises in close proximity to the Golgi and colocalises with the trans-Golgi-network protein TGN46, as well as the recycling endosome marker Rab11. This localisation pattern is not disrupted in MYO1C-mutants that do not bind actin, suggesting that the lipid-binding pleckstrin homology domain of MYO1C facilitates its Golgi association. Interestingly, the Golgi decompaction and fragmentation observed upon MYO1C inhibition is mimicked by loss of branched actin. Together with the observation that MYO1C localises to branched actin filaments, this suggests that MYO1C controls Golgi structure by stabilising branched actin. Finally, the authors show that MYO1C depletion slows the transport of cargo to the Golgi. This study, therefore, identifies a novel protein that regulates Golgi structure and highlights its requirement for efficient intracellular trafficking.