The human LAR (PTPRF) gene has 2 tandemly repeated PTPase associated tandem subunit domains, locus: 1p34.2 [§§;^] and represents a receptor-type PTP (EC 184.108.40.206), through cell-cell or cell–matrix interactions processed into 2 noncovalently associated subunits RPTPs that acts as a protein-tyrosine phosphatase associate with Trk protein tyrosine kinase (PTK) receptors in the cytoplasmic segment for dephosphorylation of tyrosine-phosphorylated insulin receptor phosphorylated by insulin stimulation. LAR is a member of the PPFIA1 (liprin) family shown to interact with PTPRF. PTP-LAR functional cell adhesion molecule (CAMs) domain 1 (cadherin and the cytoplasmic catenins) negatively regulates dephosphorylation in part of a complex (a region of the receptor-linked PTPases, absolutely required for LCA and LAR) of proteins (Trio/DAPK) that constitute adherens junctions (AJs), the generally inactive (D2) extracellular cytoplasmic domain two only decreases insulin receptor mediated autophosphorylation, a process called transcytosis. The PTPRF and CD45 molecule have both domains in the cytoplasmic segment. Trio (triple functional domain (PTPRF interacting)) contains three enzyme domains: 2 that forms a complex with the cytoplasmic segments of LAR protein and a cell adhesion-like ectodomain. LAR (PTPRF) is widely expressed in receptor-type protein-tyrosine-phosphatases as a regulator of insulin receptor (IR). Liprin localize LAR to cell focal adhesions-like ectodomain, the laminin–nidogen complex is a ligand for a coiled-coil LAR-interacting protein where PPFIA1 co-localizes. LAR is important for dendrite development.