{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nRIPK4 is a serine/threonine kinase that plays a central role in regulating epidermal differentiation, keratinocyte development, and barrier formation. Its activity promotes the phosphorylation and activation of transcription factors such as IRF6, thereby orchestrating gene expression programs critical for proper epithelial maturation. Mutations in RIPK4 underlie congenital syndromes—including Bartsocas‐Papas and CHAND—that are characterized by craniofacial, limb, and cutaneous defects, and its modulation of Wnt/β‐catenin signaling further supports its essential function in normal skin development and immune regulation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "11"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its developmental role, RIPK4 exerts multifaceted effects in oncogenesis across diverse malignancies. Aberrant expression or mutation of RIPK4 has been linked to enhanced tumor cell proliferation, migration, and invasion in cancers such as diffuse large B‐cell lymphoma, hepatocarcinogenesis, cervical, pancreatic, nasopharyngeal, lung, osteosarcoma, ovarian, and melanoma. Mechanistically, dysregulated RIPK4 can activate key signaling cascades—including NF‐κB, Wnt/β‐catenin, IL‐6/STAT3, TGF‐β, and pathways involving protein kinase C isoforms—to promote epithelial–mesenchymal transition, alter cell adhesion, and support a pro‐inflammatory tumor microenvironment. In some contexts, loss of RIPK4 function appears to drive dedifferentiation and contribute to a more aggressive phenotype, underscoring its context‐dependent role as either an oncogene or tumor suppressor."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "27"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nRecent mechanistic studies have detailed the complex post‐translational regulation of RIPK4 that fine‐tunes its cellular functions. Activated RIPK4 is targeted for K48‐linked ubiquitination by the SCFβ–TrCP E3 ligase, a process that is counteracted by deubiquitinases such as UCHL3—whose association is enhanced by GSK3β‐mediated phosphorylation of RIPK4. Such modifications not only control the stability and expression level of RIPK4 but also, in turn, modulate downstream signaling through NF‐κB, Wnt/β‐catenin, and TGF‐β pathways. These insights into RIPK4’s regulation help to explain its dual roles in supporting normal epithelial homeostasis while also contributing to tumor progression and inflammatory responses."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "28"}, {"type": "fg_f", "ref": "16"}, {"type": "fg_f", "ref": "26"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Stewart T Moran, Khaleda Haider, Yongkai Ow, et al. 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