Epithelial cells are characterized by a junctional complex, which consists of tight junctions (TJ), adherens junctions (AJ) and desmosomes (D). The junctional complex is formed by both integral membrane proteins, which allow adhesion and form a paracellular barrier, and cytoplasmic proteins, which connect transmembrane proteins to the cytoskeleton and have signalling functions. Understanding how the junctional complex is assembled and regulated is of fundamental importance for epithelial physiology. Paracingulin is a cytoplasmic protein of TJ and AJ, which regulates the activity of small GTPases, RhoA and Rac1. In this work we characterize the molecular interactions of paracingulin at epithelial junctions, and show that paracingulin forms a complex with ZO-1, cingulin, E-cadherin, PLEKHA7 and p120ctn. We provide the first characterization of expression and tissue distribution of PLEKHA7, a paracingulin-binding protein, and we demonstrate that PLEKHA7 recruits paracingulin to AJ, whereas ZO-1 targets paracingulin to TJ.