PTPR

PTPR stands for protein tyrosine phosphatase receptor, a family of receptor-type protein tyrosine phosphatases (RPTPs) that regulate cellular signaling by removing phosphate groups from tyrosine residues on target proteins. These enzymes are part of the broader protein tyrosine phosphatase superfamily and play key roles in controlling signals that govern cell behavior.

Structurally, PTPRs are single-pass transmembrane proteins. They typically feature an extracellular domain, which can include immunoglobulin-like and fibronectin type III modules, a single transmembrane helix, and one or two intracellular phosphatase domains. In most members, the first phosphatase domain (D1) is catalytically active, while the second (D2) is regulatory or inactive. This arrangement enables extracellular cues to influence intracellular phosphatase activity and downstream signaling.

Functionally, PTPRs regulate processes such as cell adhesion, migration, proliferation, differentiation, and neural development. By dephosphorylating substrates associated with receptor tyrosine kinases, integrins, or cytoskeletal components, they modulate signaling pathways including MAPK and PI3K-Akt. Their activities can either suppress or promote tumorigenesis depending on cellular context and interacting partners.

In humans, several PTPR genes are recognized, including PTPRA, PTPRB, PTPRD, PTPRG, PTPRJ, PTPRS, and PTPRZ1. Expression patterns are tissue- and development-stage dependent, and individual family members can have distinct as well as overlapping roles.

PTPRs are studied for their involvement in development, cancer, and nervous system function, making them an active area of biomedical research.