LRRK2 is a large, multidomain protein. Mutations in LRRK2 gene account for up to 13% of familiar Parkinson's disease cases. Despite intense research efforts, information on the physiological and pathological function(s) of LRRK2 is still fragmentary. Since LRRK2 contains an enzymatic core composed of a GTPase and a kinase domain, it is thought to act as a signaling molecule. Furthermore, the primary structure of LRRK2 includes several domains that are predicted to function in protein-protein interactions. To shed more light on LRRK2 signaling pathways, we used a high throughput approach to search for binding partners. Highly pure LRRK2 protein was probed against 9000 recombinant proteins linked to a solid surface in a Protoarray. One of the most promising LRRK2 interactors is p21-activate kinase 6 (PAK6), a brain-specific dimeric kinase implicated in the regulation of cell morphology and cytoskeleton rearrangements. Here, we validate the interaction between the two proteins by co-immunoprecipitation and immunocytochemistry. Interestingly, in HEK293T cell model the two kinases co-localize and are associated with filamentous peripheral structures positive to F-actin staining. In this frame we are also investigating the role of PAK6 expression level on LRRK2 phosphorylation status. In conclusion, our results point to PAK6 as a novel LRRK2 interactor and suggest a potential role of the LRRK2-PAK6 complex on the regulation of cytoskeleton dynamics.