Receptor protein tyrosine phosphatase mu (PTPRM)

Receptor protein tyrosine phosphatase mu (PTPRM) is a member of the type IIB subfamily of receptor-like tyrosine phosphatases that plays a critical role in mediating cell-cell adhesion through homophilic interactions (UniProt P28658; PMID: 15254213). It consists of an extracellular domain with an immunoglobulin-like domain and fibronectin type III repeats, and an intracellular portion containing two catalytic phosphatase domains (UniProt P28658). PTPRM is known to regulate the phosphorylation state of cadherin-catenin complexes, thereby stabilizing adherens junctions and influencing signal transduction pathways related to cell growth and migration (PMID: 24121272; PMID: 15254213). In various cancers, particularly glioblastoma and colorectal cancer, PTPRM expression is frequently downregulated or the protein is proteolytically cleaved, which contributes to increased tumor cell invasion and metastasis (PMID: 24121272; PMID: 30333295). Consequently, PTPRM is being investigated as a therapeutic target and a diagnostic biomarker, with research focusing on peptides that mimic its extracellular domain to inhibit tumor cell migration or serve as targeted imaging agents (PMID: 30333295). Its involvement in vascular integrity also suggests potential roles in treating inflammatory and cardiovascular conditions (PMID: 24121272).

Other names

Protein tyrosine phosphatase receptor type MPTP muRPTP-muPTPMR-PTP-mu

Experimental agents target the extracellular domain of PTPRM to mimic or disrupt homophilic binding, which modulates intracellular signaling pathways and inhibits the invasive behavior of tumor cells by stabilizing cell-cell junctions (PMID: 30333295).