Target intelligence / Profile preview

Fidgetin-like protein 1 (FIGNL1)

Target
FIGNL1
Molecular classification
AAA+ ATPase protein family, Microtubule-severing protein (probable, based on homology and some functional studies), Centrosome protein
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Overview

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].

Other names
FIGL-1Fidgetin like 1Fignl1 (gene symbol)
02

Mechanism of action

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

03

Biological functions

DNA double-strand break repair via homologous recombinationRegulation of RAD51 chromatin associationNegative regulation of ciliogenesisMicrotubule severing and cytoskeletal regulationCentrosome and centriole-associated cellular functions
04

Disease associations

Cancer (mutations found in various cancer types)Genetic disorders (essential gene in mice, mutations cause developmental defects)Ciliopathies (based on phenotypic similarity in animal models)Genome instability-associated diseases
05

Safety considerations

Potential for adverse effects on genome stability if inhibited or dysregulated (as protein is essential for DNA double-strand break repair and mitotic progression)Possible impact on cilia formation and function, relevant in developmental and ciliopathy contexts

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