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Fidgetin-like protein 1 (FIGNL1) is an AAA+ ATPase family protein involved in the regulation of critical cellular processes, including homologous recombination repair of DNA double-strand breaks and the modulation of microtubule networks. FIGNL1 interacts with and remodels RAD51, controlling its association with chromatin and thereby maintaining genome stability. In addition to its nuclear functions, FIGNL1 localizes to the centrosome—specifically, the mother centriole—where it regulates ciliogenesis by inhibiting primary cilium assembly via its ATPase and probable microtubule-severing activity. Disruption of FIGNL1 is associated with genomic instability, developmental anomalies, cancer, and ciliopathy-like syndromes. Although it is not yet an established pharmacological target, its central role in genome maintenance and cell structure suggests considerable biological and potential therapeutic interest[1][2][3][4][5].
No drugs reported, but Fignl1 mechanistically acts by: - Promoting dissociation of RAD51 from chromatin (critical for DNA repair regulation) - Severing or reorganizing microtubule networks, possibly through ATP-dependent remodeling
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