{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nProtein‐tyrosine phosphatase nonreceptor type 3 (PTPN3), also known as PTPH1, is a multidomain enzyme harboring FERM, PDZ, and catalytic domains that orchestrates diverse signaling processes in normal physiology. It regulates receptor functions by, for example, modulating ectodomain shedding through its action on the metalloprotease TACE, dephosphorylating immune receptor components such as the T cell receptor ζ chain, and fine‐tuning ion channel activity via interaction with Na(v)1.5. In addition, PTPN3 plays a role in the control of growth hormone receptor signaling by affecting insulin‐like growth factor expression."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "4"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nDysregulation of PTPN3 is strongly implicated in cancer pathogenesis, with context‐dependent roles that span tumor suppression to oncogenic promotion. Viral oncoproteins—including those from high‐risk human papillomaviruses (HPV)—bind to and promote the degradation of PTPN3, thereby subverting its phosphatase functions."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "5"}]}, {"type": "t", "text": " Moreover, PTPN3 dephosphorylates key substrates such as p38γ MAPK to cooperate with Ras signaling"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "7"}]}, {"type": "t", "text": ", while in breast cancer it modulates vitamin D receptor expression to stimulate tumor growth."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "8"}]}, {"type": "t", "text": " Genomic alterations, including fusion events observed in non‐small cell lung carcinoma and mutations identified in intrahepatic cholangiocarcinoma, further emphasize its tumor‐suppressive potential."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "9"}]}, {"type": "t", "text": " In addition, its activity in dephosphorylating estrogen receptor tyrosine residues"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "11"}]}, {"type": "t", "text": ", together with reports of mutations and altered expression in cholangiocarcinoma"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "12"}]}, {"type": "t", "text": ", NSCLC"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "13"}]}, {"type": "t", "text": ", ovarian cancer"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "14"}]}, {"type": "t", "text": ", breast cancer"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "15"}]}, {"type": "t", "text": ", glioblastoma"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "16"}]}, {"type": "t", "text": ", and even in promoting lung cancer cell motility via Src/DAAM1 signaling"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "17"}]}, {"type": "t", "text": ", underscores its multifaceted and sometimes paradoxical functions in tumorigenesis.\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond these roles in oncogenesis, PTPN3 is critically involved in host–virus interactions and the regulation of the tumor microenvironment. In keratinocytes, for instance, binding of HPV8 E6 enhances PTPN3’s protein levels and phosphatase activity, thus promoting cell proliferation."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "18"}]}, {"type": "t", "text": " In addition, while studies in perihilar cholangiocarcinoma provide a rationale for further exploration of its expression"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "19"}]}, {"type": "t", "text": ", microRNA‐mediated targeting of PTPN3 in gastric cancer leads to augmented MAPK phosphorylation and angiogenesis."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "20"}]}, {"type": "t", "text": " Furthermore, PTPN3 expression is upregulated by NFκB in activated lymphocytes—an effect linked to immune checkpoint regulation—and its suppression has been shown to alleviate lymphocyte exhaustion and improve anti–PD‑1 therapeutic efficacy."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "21"}]}, {"type": "t", "text": " Structural studies have provided insights into how its PDZ domain mediates interactions with viral proteins and endogenous substrates"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "23"}]}, {"type": "t", "text": ", and emerging evidence in pancreatic cancer"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "24"}]}, {"type": "t", "text": "as well as analyses of its role in drug sensitivity and the tumor immune microenvironment"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "25"}]}, {"type": "t", "text": "further attest to its significance as both a prognostic biomarker and a potential therapeutic target.\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Yufang Zheng, Johannes Schlondorff, Carl P Blobel "}, {"type": "b", "children": [{"type": "t", "text": "Evidence for regulation of the tumor necrosis factor alpha-convertase (TACE) by protein-tyrosine phosphatase PTPH1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M207459200"}], "href": "https://doi.org/10.1074/jbc.M207459200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12207026"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12207026"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Margaret S Sozio, Meredith A Mathis, Jennifer A Young, et al. 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