{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPTPRZ1 (also known as receptor‐type protein tyrosine phosphatase β/ζ) plays a prominent role in the central nervous system. In normal development and repair it contributes to oligodendrocyte survival and remyelination in demyelinating diseases such as multiple sclerosis, and its expression is induced during nigrostriatal development and in remyelinating oligodendrocytes. PTPRZ1 also participates in neural cell recognition through its interactions with molecules such as the contactins, and its signaling influences stem cell maintenance in neural progenitors and human embryonic stem cells. Moreover, although genetic studies in autism did not reveal a major causative role, enhanced PTPRZ1 signaling has been linked to neurodevelopmental and psychiatric alterations including schizophrenia."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "12"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the context of cancer, particularly gliomas and other solid tumors, PTPRZ1 is frequently upregulated or rearranged to form oncogenic fusion proteins such as the PTPRZ1‐MET (ZM) fusion. These alterations potentiate signaling pathways that enhance cell migration, invasion, epithelial–mesenchymal transition and stem cell–like properties, thereby contributing to tumor progression and poor clinical outcome in glioblastoma and other cancers (including breast, prostate, colorectal and renal carcinomas). In addition, PTPRZ1 acts as the receptor for ligands such as pleiotrophin (PTN) and heparin affin regulatory peptide (HARP), which inactivate its phosphatase activity to promote downstream pro‐migratory signaling and angiogenesis. Structural and biochemical studies further detail how PTPRZ1 regulates substrate phosphorylation (for example of focal adhesion effectors) and how its interactions—whether via direct binding or fusion events—fuel oncogenic output."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "13", "end_ref": "38"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMoreover, the regulatory complexity of PTPRZ1 is underscored by its post‐translational modification and proteolytic processing, which modulate its cellular localization and signaling output. Ligand binding by PTN, HARP or interleukin‑34 can induce receptor clustering and transient inactivation of phosphatase activity, thereby facilitating oncogenic kinase activation (such as that of ALK or MET) and downstream signaling alterations. The therapeutic targeting of the PTN–PTPRZ1 axis as well as the detection of PTPRZ1 fusion proteins in patient specimens are emerging strategies that promise to improve diagnosis and intervention in glioma and other cancers."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "18"}, {"type": "fg_f", "ref": "30"}, {"type": "fg_fs", "start_ref": "33", "end_ref": "38"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Sheila Harroch, Glaucia C Furtado, Wolfgang Brueck, et al. 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