Vesicular trafficking and cargo delivery require the specific fusion of a transport vesicle with a distinct target membrane. Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins are thought to mediate almost all cellular membrane fusion events, and fusion along endocytic pathways is known to depend directly on the proper distribution of SNAREs. In this paper (p. 3745), Marko Jović, Tamas Balla and colleagues explore a central cellular mechanism for the subcellular distribution of SNAREs along the endomembrane system, focusing specifically on the small R-SNARE vesicle-associated membrane protein 3 (VAMP3), which is involved in recycling and retrograde transport. The authors identified the lipid kinase phosphatidylinositol 4-kinase IIα (PI4K2A) as a binding partner of VAMP3, and demonstrated colocalisation of the two proteins on tubulo-vesicular endosomes. VAMP3 was then shown to regulate the subcellular distribution of PI4K2A. Knockdown of PI4K2A led to missorting of VAMP3, and impaired its ability to form a fusion complex with its cognate Q-SNARE; moreover, the rate of VAMP3-mediated recycling of the transferrin receptor was impaired. Kinase activity did not affect PI4K2A binding to VAMP3, but depletion of phosphatidylinositol 4-phosphate reduced the rate at which VAMP3 appeared at the target membrane. This body of work therefore describes a new interaction between PI4K2A and VAMP3 that is important in the sorting and localisation of both proteins.