Cilia have been associated with diverse developmental and physiological processes, and defects in cilia underlie a number of genetic conditions. Several lines of evidence support a critical role of the actin cytoskeleton in ciliogenesis and ciliary function. Here, we show that well-characterized focal adhesion (FA) proteins, including FAK, Paxillin, and Vinculin, associate with the basal bodies of multiciliated cells and form complexes (CAs) that interact with the actin cytoskeleton. FAK downregulation leads to ciliogenesis defects similar to those observed when the actin cytoskeleton is disrupted, including defects in basal body migration, docking, and spacing, suggesting that CAs link basal bodies to the actin cytoskeleton. The important role of FA proteins in ciliogenesis leads us to propose that evolutionarily FA proteins, many of which are found in primitive flagellated unicellular eukaryotes, may have originally evolved to perform functions at flagella and were later co-opted for use in cell adhesion. •Focal adhesion proteins associate with the basal bodies in ciliated cells•FAK, Paxillin, and Vinculin form “ciliary adhesion” complexes•Ciliary adhesions link basal bodies to the actin cytoskeleton•Downregulation of FAK leads to defects in ciliogenesis Antoniades et al. show that focal adhesion proteins FAK, Paxillin, and Vinculin form “ciliary adhesion” (CA) complexes that associate with basal bodies and interact with the actin cytoskeleton. FAK disruption results in ciliogenesis defects, suggesting that CAs connect basal bodies to the actin cytoskeleton, a key modulator of motile ciliogenesis.