Huntingtin (HTT), the protein responsible for Huntington’s disease (HD), is ubiquitously expressed and enriched in neurons. HTT associates with microtubule motors, kinesin-1 and dynein, and is involved in the movement of vesicles within axons. However the type of vesicle or cargo complex that HTT transports within axons is unknown. We previously found that reduction of Drosophila HTT perturbed the movement of Rab4 GTPase- containing vesicles in larval axons. Simultaneous dual‐view imaging revealed that HTT and Rab4 likely move together within Drosophila larval axons. Sub-pixel co-localization analysis revealed that Rab4, HTT, and motor proteins co-localize suggesting that a HTT-motor complex likely exists in vivo. Reduction of the huntingtin interacting protein 1 (HIP1) and a known Rab effector, Rip11, perturbed the movement of both HTT and Rab4 in vivo. However, reduction of Milton (a protein with some sequence homology to HAP1) and Nemo (a Rab8 effector) had no effect. Taken together, our observations suggest that HIP1 and Rip11 may aid in linking HTT-Rab4-containing complexes to motor proteins. Since expansion of poly-glutamine repeats in the context of human HTT perturbed the motility of Rab4, perhaps HTT normally functions to facilitate Rab4 motility within axons for functions at the synapse.