Receptor-type tyrosine-protein phosphatases

Like neurexins, Receptor-like protein tyrosine phosphatases (RPTPs) make trans-synaptic adhesion complexes with multiple postsynaptic binding partners to regulate synapse organization. The type IIa RPTPs include three members, Receptor-type tyrosine-protein phosphatase F (PTPRF) sometimes referred to as leukocyte common antigen-related (LAR), Receptor-type tyrosine-protein phosphatase sigma (PTPRS) and Receptor-type tyrosine-protein phosphatase delta (PTPRD). These proteins contain typical cell adhesion immunoglobulin-like (Ig) and fibronectin III (FNIII) domains, suggesting the involvement of RPTPs in cell-cell and cell-matrix interactions. To date, six different types of postsynaptic organizers for type-IIa RPTPs have been reported: interleukin-1 receptor accessory protein (IL1RAP, IL-1RAcP), IL-1RAcP-like-1 (IL1RAPL1), Neurotrophin receptor tyrosine kinase 3 (NTRK3, TrkC), Leucine-rich repeat-containing protein 4B (LRRC4B, Netrin-G ligand-3, NGL-3), the Slit- and Trk-like (Slitrk) family proteins and the liprins.

Summary from Reactome (R-HSA-388844), read 2026-09-23.