ArticleMolecular biology of the cell2025
Trimerization domain-interfering peptide inhibits EML4-ALK condensate formation, fusion-dependent signaling, and cell growth.
Article in Molecular biology of the cell, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed.
- Fusion protein condensate formation via coiled-coil domains.Protein science : a publication of the Protein Society · 2026Article
- Alphaviral Capsid Proteins Inhibit Stress Granule Assembly via Competitive RNA Binding With G3BP1.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Pharmacological targeting of oncogenic condensates in cancer: mechanistic insights and therapeutic opportunities.Acta pharmacologica Sinica · 2026Review
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8 authors.
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Abstract
Biomolecular condensates are micrometer-scale subcellular structures assembled through protein phase separation in living cells. Recent research shows that they are critical to normal biological processes and their misregulation may contribute to disease. A prominent example is the cancer-causing EML4-ALK fusion protein, which spontaneously forms biomolecular condensates that significantly enhance receptor tyrosine kinase (RTK) signaling within the condensate microenvironment. In this work, we show that a trimerization domain (TD) in EML4-ALK is necessary for condensate formation. By designing a peptide targeting the TD, we disrupted EML4-ALK self-assembly, leading to the dissolution of pre-existing EML4-ALK condensates in patient lung tumor-derived cells. Notably, this disruption significantly reduced EML4-ALK-dependent signaling and cell proliferation. Our findings demonstrate that interfering with a specific protein-protein interaction can disrupt oncogenic biomolecular condensates and attenuate their associated signaling. These results highlight the potential of targeting condensate assembly as a strategy to modulate oncogenic signaling.
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