ArticleBiology2026
JAK3-Mediated Structural Remodeling of β-Catenin Suppresses Epithelial-Mesenchymal Transition: Insights from In Silico Modeling.
Article in Biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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3 authors.
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Abstract
introductionJanus kinase 3 (JAK3) is a non-receptor tyrosine kinase that phosphorylates multiple proteins, including β-catenin, a critical component of adherens junctions (AJs). We previously demonstrated that JAK3-mediated phosphorylation of β-catenin regulates its basolateral localization and preserves epithelial barrier integrity. However, the structural basis underlying JAK3-β-catenin interactions and their role in epithelial-mesenchymal transition (EMT) remains unclear. METHODOLOGY: Here, we employed homology modeling, molecular docking, and structural simulations to investigate phosphorylation-dependent interactions between JAK3 and β-catenin.
resultsOur analysis revealed that Src-mediated phosphorylation at Y654 induces conformational remodeling of the β-catenin N-terminal domain (NTD), creating a favorable interface for JAK3 binding and shifting its interaction from the armadillo repeat domain to the NTD. Subsequent JAK3-mediated phosphorylation at Y30, Y64, and Y86 restores β-catenin conformation, stabilizes the E-cadherin/β-catenin complex, and limits nuclear translocation. Phosphomimetic analyses identified distinct structural contributions of these residues.
conclusionsCollectively, these findings reveal a sequential Src-JAK3 phosphorylation mechanism that maintains AJ integrity and suppresses EMT, providing potential therapeutic insights into epithelial cancer progression.
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