Filamin A interacting protein 1-like (FILIP1L) is a multifunctional protein that plays a role in cancer progression, apoptosis, and angiogenesis. However, FILIP1L remains a relatively underexplored protein, and many of FILIP1L’s key mechanisms and interacting partners are still unknown. Using immunofluorescence staining for endogenous FILIP1L and high-resolution confocal microscopy, we show that FILIP1L colocalizes with the mitochondrial marker, TOM20, suggesting a novel connection between FILIP1L and mitochondria. Further exploring the relationship between FILIP1L and mitochondria might provide a deeper understanding of the emerging function of FILIP1L in health and disease.