May play a structural role at sites of cell adhesion in maintaining cell shape and motility. In addition to these structural functions, it may also be implicated in signaling events and activation of gene transcription. May be involved in signal transduction from cell adhesion sites to the nucleus allowing successful integration of signals arising from soluble factors and cell-cell adhesion sites. Also suggested to serve as a scaffold protein upon which distinct protein complexes are assembled in the cytoplasm and in the nucleus. Interacts with VASP, with PDZ domains of SCRIB and with ACTN1/alpha-actinin. Found in the nucleus, in the cytoplasm and at cell adhesion sites. Shuttles between the cytoplasm and the nucleus. It has been found in sites of cell adhesion such as cell-to-cell contact and focal adhesion which are membrane attachment sites of cells to the extracellular matrix. Mainly nuclear when fused with HMGA2/HMGIC and KMT2A/MLL1. Expressed in a wide variety of tissues but no or very low expression in brain and peripheral leukocytes. A chromosomal aberration involving LPP is associated with a subclass of benign mesenchymal tumors known as lipomas. Translocation t(3;12)(q27-q28;q13-q15) with HMGA2 is shown in lipomas. A chromosomal aberration involving LPP is associated with pulmonary chondroid hamartomas. Translocation t(3;12)(q27-q28;q14-q15) with HMGA2 is detected in pulmonary chondroid hamartomas. A chromosomal aberration involving LPP is associated with parosteal lipomas. Translocation t(3;12)(q28;q14) with HMGA2 is also shown in one parosteal lipoma. A chromosomal aberration involving LPP is associated with acute monoblastic leukemia. Translocation t(3;11)(q28;q23) with KMT2A/MLL1 is associated with acute monoblastic leukemia. Belongs to the zyxin/ajuba family.