Many cancer cells or transformed fibroblasts make invadopodia, which are actin-rich adhesive organelles that are capable of remodeling the extracellular matrix. Invadopodia, and closely related podosomes, facilitate cell migration and invasion through the tissues. Recently, it was shown that Amotl2 plays a crucial role in invadopodia formation in Src-transformed fibroblasts by regulating actin cytoskeleton organization. One function of Amotl2 is regulation of the Hippo signaling pathway through the interaction with YAP transcription co-activator. Actin-associated Amotl2 sequesters cytoplasmic YAP and inhibits its nuclear translocation and transcription of Hippo-dependent genes. In this study, we investigated localization of YAP in Src-3T3 cells and observed that this protein concentrates at actin-rich invadopodia. This result suggests that YAP is a novel invadopodia component and may regulate organization of these organelles.