{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nReceptor protein tyrosine phosphatase α (PTPRA) is emerging as a multifunctional regulator whose dysregulation impacts cancer biology and microbial pathogenesis. For example, a circular RNA derived from the PTPRA gene (circPTPRA) has been implicated in non‐small cell lung carcinoma development"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": ", while PTPRA itself serves as a receptor for Helicobacter pylori VacA toxin, triggering vacuolation and apoptotic responses in gastric epithelial cells."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": " In prostate cancer, elevated levels of PTPRA contribute to neuroendocrine transdifferentiation via sustained ERK pathway activation"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": ", and in gastric as well as squamous cell lung cancers, increased expression of PTPRA is strongly associated with disease progression."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": " Moreover, expression of aberrant PTPRA splice variants has been linked to enhanced Src dephosphorylation and oncogenic transformation"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "6"}]}, {"type": "t", "text": ", and VacA‐induced Src phosphorylation that leads to CagA tyrosine phosphorylation further underscores its role in infection‐associated cellular signaling."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nPTPRA exerts much of its biological influence by modulating key tyrosine kinase activities and organizing cytoskeletal as well as adhesion complexes. Structural studies have revealed that PTPRA dimerizes with distinct conformational states that regulate its catalytic activity"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "8"}]}, {"type": "t", "text": ", and RNAi‐mediated suppression of PTPRA in multiple cancer cell lines reduces Src kinase activity."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "9"}]}, {"type": "t", "text": " Analysis of forced dimer mutants further indicates that the rotational coupling of PTPRA dimers is linked to its active state."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "10"}]}, {"type": "t", "text": " In epithelial cells, PTPRA is recruited to adherens junctions where it regulates E‐cadherin accumulation and mediates Src activation leading to proper cortactin phosphorylation."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "11"}]}, {"type": "t", "text": " Its role in modulating cellular responses to matrix forces is also evident in colon cancer cells by increasing contractility and promoting adhesion site formation."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "13"}]}, {"type": "t", "text": " In addition, PTPRA collaborates with PI 3‐kinase and PKCδ to dephosphorylate pp60(c‑Src), thereby activating the ERK/MAPK cascade in response to therapeutic agents"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "14"}]}, {"type": "t", "text": ", and biochemical studies have shown that its intracellular domains can form regulated complexes with scaffolding proteins such as liprin‐α."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "15"}]}, {"type": "t", "text": " Furthermore, growth factor–induced as well as integrin‐dependent signals control PTPRA phosphorylation (for example, via IGF‑1 and Abl in a RACK1‐dependent manner), ultimately modulating cell migration."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "16"}]}, {"type": "t", "text": " Additional evidence from studies on cell cycle regulation shows that PTPRA‐mediated Src activation is critical for the G2‑to‑mitosis transition"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "17"}]}, {"type": "t", "text": "and that its extracellular domains cooperate with the intracellular D2 domain to allosterically restrain the catalytic D1 domain."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "18"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its role in modulating kinase signaling and adhesion dynamics, PTPRA influences ion channel function and metabolic processes. Studies in heterologous cells and native tissues have demonstrated that PTPRA decreases the cell surface expression of hyperpolarization‐activated cyclic nucleotide–gated channels (HCN2), thereby regulating channel current properties."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "19"}]}, {"type": "t", "text": " In renal epithelial models, PTPRA interacts with the tetraspanin CD63 to stimulate c‑Src activity, which in turn modulates ROMK channel function"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "20"}]}, {"type": "t", "text": ", and similar principles appear to extend to its regulation of focal adhesion remodeling via Rac1 activation."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "21"}]}, {"type": "t", "text": " Moreover, in pancreatic β‑cells, overexpression of the wild‑type splice variant of PTPRA reduces insulin secretion, highlighting its negative regulatory role in metabolic signaling."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "22"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nPTPRA also plays important roles in neurodevelopment and fibrogenesis. In the central nervous system, it regulates the cell surface level of the neural adhesion molecule NB‑3, which is essential for dendrite development of cortical neurons."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "23"}]}, {"type": "t", "text": " Mouse genetic studies further implicate PTPRA in regulating radial neuronal migration and oligodendrocyte differentiation, with rare damaging variants in PTPRA being associated with increased schizophrenia risk."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "24"}]}, {"type": "t", "text": " PTPRA also contributes to inflammatory signaling at focal adhesions, where its interaction with the phosphatase SHP‑2 is critical for interleukin‑1–induced MMP3 release"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "26"}]}, {"type": "t", "text": ", and elevated plasma levels of PTPRA have been observed during fibrogenesis associated with parasitic infections."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "27"}]}, {"type": "t", "text": " Notably, microRNA‑146a‑5p can attenuate fibrosis‐related marker expression by targeting the PTPRA–Src signaling axis."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "28"}]}, {"type": "t", "text": " In addition, alternative splicing events that insert extra amino acids into the extracellular domain of PTPRA enhance its ability to activate Src‐dependent signaling"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "29"}]}, {"type": "t", "text": ", while extracellular proteolytic processing by ADAM17 further modulates its signaling potential."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "30"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Siliang Wei, Yuanyuan Zheng, Yanru Jiang, et al. 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