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Ras association domain-containing protein 10 (RASSF10) is a member of the Ras association domain family of proteins, functioning primarily as a tumor suppressor. It contains a Ras-association (RA) domain and central coiled-coil domains but lacks catalytically active domains. RASSF10 is predominantly regulated at the epigenetic level, with frequent promoter hypermethylation leading to its inactivation in numerous cancers, including hepatocellular carcinoma, lung cancer, thyroid cancer, and others. Functionally, RASSF10 inhibits cell proliferation, promotes apoptosis, and helps maintain epithelial cell characteristics by opposing epithelial-mesenchymal transition (EMT) through stabilization of E-cadherin and interaction with the apoptosis-stimulating protein of p53 (ASPP2). Loss or reduced expression of RASSF10 correlates with advanced tumor stage, invasiveness, and poor clinical outcome. No drugs are currently known to specifically target RASSF10, but its expression and methylation status are emerging as clinically relevant biomarkers[1][2][3][5][7][8].
No approved drugs currently target RASSF10 directly. Mechanistically, RASSF10 exerts tumor suppressor effects by upregulating pro-apoptotic signaling (e.g., via p53, JNK, inhibition of Wnt/β-catenin), promoting E-cadherin expression (anti-EMT), and regulating the cell cycle[1][3][8].
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