{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPTPN14 is emerging as a pivotal tumor‐suppressor molecule largely through its regulation of Hippo signaling. In multiple studies, PTPN14 has been shown to bind directly to the transcriptional co‐activator YAP via its WW and PPxY motifs, thereby promoting YAP’s cytoplasmic sequestration and inhibiting its ability to drive pro‐proliferative and anti‐differentiation gene expression. Furthermore, this phosphatase is subject to transcriptional upregulation by p53 and can be suppressed by specific microRNAs, underscoring its dynamic regulation in various cancer types—including pancreatic, prostate, glioblastoma, osteosarcoma, and breast cancer—in which its status correlates with patient outcomes."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "9"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the context of viral oncogenesis, high‐risk human papillomavirus (HPV) E7 proteins have been shown to directly bind and target PTPN14 for proteasomal degradation. This viral subversion of PTPN14 not only contributes to a reduction in LATS1 kinase activation—diminishing the inhibitory phosphorylation of YAP—but also impairs keratinocyte differentiation and enhances cellular survival. Structural studies further demonstrate that mutations in conserved residues of E7 that disrupt PTPN14 binding attenuate its transforming ability, providing a mechanistic link between HPV infection and deregulated Hippo pathway signaling."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "10", "end_ref": "14"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles in oncogenic pathways, PTPN14 also contributes to normal developmental and homeostatic processes. Genetic loss‐of‐function mutations in PTPN14 have been implicated in congenital lymphatic anomalies and vascular dysplasias, as exemplified by its involvement in lymphangiogenesis and hereditary hemorrhagic telangiectasia. Mechanistically, PTPN14 regulates cell adhesion and migration by dephosphorylating key substrates such as p130Cas, and it has been linked to the restoration of endothelial barrier function via regulation of VE‐cadherin recycling. Moreover, by dephosphorylating PDGFRβ, PTPN14 influences smooth muscle cell phenotypic modulation, while its aberrant expression or mutation has been associated with a spectrum of pathologies ranging from gingival fibromatosis and sporadic trichilemmoma to predisposition for basal cell and cervical carcinomas, as well as contributing to pro‐tumorigenic signaling through NFκB and PI3K/AKT/mTOR activation in gastric cancer."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "15", "end_ref": "27"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nCollectively, these findings position PTPN14 as a central regulatory hub whose loss or dysregulation—whether through somatic or germline alterations, post‐transcriptional suppression by microRNAs, or active degradation by viral oncoproteins—can perturb Hippo pathway activity and other signaling networks essential for cell differentiation, adhesion, and vascular homeostasis. This multifaceted functionality underscores its significance as both a tumor suppressor and a mediator of developmental processes.\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "X Liu, N Yang, S A Figel, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PTPN14 interacts with and negatively regulates the oncogenic function of YAP."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncogene (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/onc.2012.147"}], "href": "https://doi.org/10.1038/onc.2012.147"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22525271"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22525271"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Wenqi Wang, Jun Huang, Xin Wang, et al. 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