LAR, Leukocyte common antigen related, Receptor-type tyrosine-protein phosphatase F (PTPRF)

PDB-1LAR Associated subunits RPTPs (receptor protein tyr. phos.) that acts as a protein-tyrosine phosphatase Domain 1The human LAR (PTPRF) gene has 2 tandemly repeated PTPase associated tandem subunit domains, locus: 1p34.2 [§§;^] and represents a receptor-type PTP (EC 3.1.3.48), through cell-cell or cellmatrix 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)placement of tyrosine phosphorylated 1LAR that is other wise in the center between the two domains D1 and D2 here on the D1 ribbon 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 lamininnidogen complex is a ligand for a coiled-coil LAR-interacting protein where PPFIA1 co-localizes. LAR is important for dendrite development.

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