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Centrosomal protein 20 (CEP20) is a conserved LisH domain-containing protein localized to centrioles and centriolar satellites within the centrosome, where it participates in the regulation of microtubule dynamics, cilium assembly, and cell cycle progression, particularly S-phase control. CEP20 recruits polo-like kinase 1 (PLK1) to the centrosome, a process critical for normal DNA replication and cell division. CEP20 is implicated in essential developmental and cellular processes, with evidence for roles in embryonic patterning, angiogenesis, and ciliogenesis. Increased CEP20 expression is strongly correlated with enhanced proliferation, migration, and metastatic potential in non-small cell lung cancer; its downregulation impairs these malignant properties and disrupts microtubule polymerization dynamics. Mutations or dysfunction in CEP20 have also been linked to other diseases, including retinitis pigmentosa and pseudoxanthoma elasticum. CEP20 itself is not directly targeted by marketed drugs, but its regulatory role in microtubule dynamics functionally connects it to agents that perturb microtubules, such as paclitaxel.
Not directly targeted by current drugs; however, microtubule-targeting drugs (like paclitaxel) disrupt processes regulated by CEP20 (microtubule stability/dynamics)
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