Receptor-type tyrosine-protein phosphatase F (PTPRF)

Receptor-type tyrosine-protein phosphatase F (PTPRF, also known as LAR) is a transmembrane enzyme of the protein tyrosine phosphatase (PTP) family, involved in dephosphorylating tyrosine residues on target proteins and regulating diverse cellular processes such as cell growth, differentiation, adhesion, and signal transduction. Its extracellular region features three Ig-like domains and nine additional domains reminiscent of neural cell adhesion molecules, indicating a potential role in contact-mediated signaling. PTPRF’s primary functions include modulation of adherens junctions, regulation of beta-catenin signaling, and control over insulin signaling pathways. Overexpression has been observed in insulin-resistant states and may contribute to metabolic disease. Mutations and altered expression of PTPRF have also been observed in several tumor types, making it a potential therapeutic target for cancer and metabolic disease research, although no targeted therapies are currently approved[1][3][4][5].

Other names

LARBNAH2Leukocyte antigen-relatedLCA-homologreceptor-type protein-tyrosine phosphatase LARprotein tyrosine phosphatase, receptor type, F polypeptideprotein tyrosine phosphatase receptor type Fleukocyte common antigen relatedreceptor-linked protein-tyrosine phosphatase LAR

Inhibitors act by blocking the tyrosine phosphatase active site, interfering with dephosphorylation signaling and downstream pathways