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Plant cell organelles are highly motile and their positioning plays key roles in plant growth and development and responses to changing environmental conditions. Movement of organelles relies on the actin cytoskeleton and on myosins, the associated motor proteins. Myosins are suggested to bind to receptors and adaptors on organelle membranes allowing them to move on actin filaments in a step-wise manner. Despite controlling the dynamics of several organelles, the myosins and myosin receptors identified so far in Arabidopsis thaliana generally do not localise to the organelles whose movement they control, raising the issue of how specificity is determined. Our group have isolated a family of potential myosin receptors (MyoB). Here I show that unlike other members from the same family, the myosin receptor AtMRF7 specifically localises to Golgi due to the targeting information contained within its C-terminal region. MRF7 causes the class XI myosins known to affect Golgi movement, XI-K and MYA1, to relocate to the Golgi, linking these myosins for the first time to a specific compartment. MRF7 doesn’t affect the localisation of a myosin not linked to Golgi dynamics. Furthermore, FRET-FLIM confirmed the in vivo interaction between MRF7 and the myosin XI-K globular tail, showing this interaction takes place via the MRF7 N-terminal predicted myosin binding domain, DUF593. I also show that the full-length and truncated constructs of MRF7 affect, to different extents, Golgi and peroxisome dynamics. This study provides evidence that myosins from class XI can localise to organelles whose movement they control. I present a model for Golgi dynamics driven by a heterogeneous myosin population regulated through adaptor/receptor complexes.