Receptor-type tyrosine-protein phosphatase mu (PTPRM) (PTPRM)

Receptor-type tyrosine-protein phosphatase mu (PTPRM), also known as PTPmu, is a member of the Type IIB receptor protein tyrosine phosphatase family that mediates homophilic cell-cell adhesion through its extracellular domain (UniProt P28658). In healthy tissues, PTPRM stabilizes cell-cell junctions by regulating the phosphorylation state of cadherin-catenin complexes. However, in various cancers, particularly glioblastoma, PTPRM undergoes extensive proteolytic processing (shedding) by proteases such as ADAMs and gamma-secretase (Phillips-Mason et al., 2011). This cleavage results in the release of extracellular fragments into the tumor microenvironment and the generation of a truncated, pro-migratory intracellular fragment. These proteolyzed extracellular fragments serve as unique biomarkers and therapeutic targets, as they are highly prevalent in the invasive front of tumors compared to normal tissue (Burden-Gulley et al., 2010). Experimental agents, such as the SBK2 peptide, have been developed to specifically bind these fragments or the resulting neo-epitopes for tumor imaging and targeted drug delivery (Brady-Kalnay et al., 2010).

Other names

PTPmuPTP muProtein tyrosine phosphatase receptor type MR-PTP-muPTP-MAM

Targeting of neo-epitopes or fragments generated by the proteolytic cleavage of the PTPmu extracellular domain to deliver diagnostic or therapeutic payloads to tumor cells (Brady-Kalnay et al., 2010).