{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPKP1 is a key component of desmosomes that orchestrates robust cell–cell adhesion through the recruitment and stabilization of desmosomal proteins. Multiple studies have shown that loss‐of‐function mutations in PKP1 lead to a reduction in both desmosome size and number, disrupt the transition from calcium‐dependent to calcium‐independent adhesion, and cause the skin fragility–ectodermal dysplasia phenotype. Structural investigations have further revealed that its armadillo repeat domain, including unexpected insertions, serves as a critical binding interface for desmosomal partners, thereby underpinning proper desmosome assembly and keratinocyte cohesion."}, {"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": "\nIn addition to its adhesive function at intercellular junctions, PKP1 also localizes to the nucleus and cytoplasm, where it plays an unexpected regulatory role in gene expression. Notably, PKP1 directly associates with eukaryotic translation initiation factor 4A1 (eIF4A1) to stimulate its ATPase activity, thereby enhancing cap‐dependent translation. Moreover, PKP1 has been identified as a component of mRNA ribonucleoprotein complexes, suggesting that it contributes to the post‐transcriptional stabilization of transcripts encoding desmosomal proteins."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "14"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nPKP1’s functions are further modulated by post‐translational modifications and context‐dependent signal transduction pathways. Growth factor stimulation, for instance, induces Akt2‐mediated phosphorylation of PKP1, a modification that can switch its role from reinforcing desmosomal adhesion toward promoting cytoplasmic signaling activities that enhance translation and proliferation. In developmental contexts, such as tooth morphogenesis, PKP1 is upregulated and undergoes nuclear translocation in response to Wnt signaling, thereby regulating dental epithelial cell proliferation, differentiation, and tight junction composition."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "15", "end_ref": "17"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nDeregulation of PKP1 expression is tightly linked to tumor biology. Altered PKP1 levels—with reductions observed in high‐grade prostatic, esophageal, and head and neck carcinomas, and overexpression in squamous cell and lung cancers—implicate its dual roles in either suppressing or promoting tumor progression. Mechanistically, PKP1 interacts with various regulatory proteins such as NUPR1, PADI4, and RYBP, modulating oncogenic pathways including MYC translation, inflammatory cytokine stabilization, and epithelial–mesenchymal transition. These context‐dependent effects underscore the potential prognostic and therapeutic relevance of PKP1 in diverse cancers."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "18", "end_ref": "30"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its roles in adhesion, translation, and signaling, genetic studies have uncovered associations between PKP1 variants and neuropsychiatric conditions such as panic disorder, suggesting broader implications of PKP1 in cellular signaling beyond epithelial tissues."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "31"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "T Hamada, A P South, Y Mitsuhashi, et al. 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