The zyxin family of proteins consists of five members, ajuba, LIMD1, LPP, TRIP6 and zyxin, which localize at cell adhesion sites and shuttle to the nucleus. Previously, we established that LPP interacts with the tumor suppressor Scrib, a member of the leucine-rich repeat and PDZ (LAP) family of proteins. Here, we demonstrate that Scrib also interacts with TRIP6, but not with zyxin, ajuba, or LIMD1. We show that TRIP6 directly binds to the third PDZ domain of Scrib via its carboxy-terminus. Both proteins localize in cell-cell contacts but are not responsible to target each other to these structures. In the course of our experiments, we also characterized the nuclear export signal of human TRIP6, and show that LIMD1 is localized in focal adhesions. The binding between two of zyxin's family members and Scrib links Scrib to a communication pathway between cell-cell contacts and the nucleus, and implicates these zyxin family members in Scrib-associated functions.