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Palladin is an actin‐associated protein that has been suggested to play critical roles in establishing cell morphology and maintaining cytoskeletal organization in a wide variety of cell types. Palladin has been shown previously to bind directly to three different actin‐binding proteins vasodilator‐stimulated phosphoprotein (VASP), α‐actinin and ezrin, suggesting that it functions as an organizing unit that recruits actin‐regulatory proteins to specific subcellular sites. Palladin contains sequences resembling a motif known to bind profilin. Here, we demonstrate that palladin is a binding partner for profilin, interacting with profilin via a poly proline‐containing sequence in the amino‐terminal half of palladin. Double‐label immunofluorescence staining shows that palladin and profilin partially colocalize in actin‐rich structures in cultured astrocytes. Our results suggest that palladin may play an important role in recruiting profilin to sites of actin dynamics.