Relays signals from the cell surface to the nucleus to weaken adherens junction and promote actin cytoskeleton reorganization and cell invasiveness. Involved in lysophosphatidic acid-induced cell adhesion and migration. Acts as a transcriptional coactivator for NF-kappa-B and JUN, and mediates the transrepression of these transcription factors induced by glucocorticoid receptor (By similarity). Specifically interacts with the ligand binding domain of the thyroid receptor (TR) in the presence of thyroid hormone (By similarity). Interacts (via the third LIM domain and C-terminus) with PTPN13 (via the second PDZ domain). Interacts (via the second LIM domain or via the third LIM domain plus C-terminus) with PDLIM4 (via PDZ domain). Found in a complex with PTPN13 and PDLIM4 (PubMed:10826496). Interacts with SVIL isoform 2. Interacts with LPAR2 but not other LPA receptors. Interacts with PRKAA2. Interacts with MAGI1. Interacts with SCRIB (By similarity). In case of infection, interacts with S.typhimurium protein sseI (PubMed:17095609). Shuttles between nucleus and cytoplasm. Colocalizes with actin. Highly expressed in kidney, stomach, lung, heart and testis. Low expression levels in brain, colon, thymus, pancreas and skin. Not expressed in skeletal muscle. Expressed throughout development in all embryonic stages analyzed, 10.5 days post coitum (dpc) to 18.5 dpc. In 16.5 dpc embryos highly expressed in skin, lung, thymus, duodenum and the ependymal cell layer surrounding the ventricles in brain. Highly expressed also in the salivary glands, tongue, vibrissae, choroid plexus, blood vessel walls, esophagus and midgut. Low expression levels in spinal cord, heart and liver. The LIM zinc-binding domains mediate interaction with LPAR2. Phosphorylation at Tyr-55 by SRC is required for enhancement of lysophosphatidic acid-induced cell migration. Tyr-55 is dephosphorylated by PTPN13 (By similarity). Belongs to the zyxin/ajuba family.