FIGNL1

Last update 08 May 2025

Basic Info

Synonyms

fidgetin like 1, Fidgetin-like protein 1, FIGNL1

Introduction

Involved in DNA double-strand break (DBS) repair via homologous recombination (HR). Recruited at DSB sites independently of BRCA2, RAD51 and RAD51 paralogs in a H2AX-dependent manner. May regulate osteoblast proliferation and differentiation (PubMed:23754376). May play a role in the control of male meiosis dynamic (By similarity).

100 Clinical Results associated with FIGNL1

100 Translational Medicine associated with FIGNL1

0 Patents (Medical) associated with FIGNL1

Literatures (Medical) associated with FIGNL1

01 Apr 2025·Trends in Biochemical Sciences

FIGNL1 hexamer dissociates RAD51-filament: a new mechanism

Article

Author: Kumar, Rajeev

Homologous recombination (HR) is critical for maintaining genome stability, relying on RAD51 recombinase to catalyze homology-dependent accurate DNA repair. While various cellular modulators control HR, Carver, Yu, et al. reveal a unique molecular mechanism used by FIDGETIN-LIKE-1 (FIGNL1) that dissociates RAD51 from DNA through RAD51 N terminus and FIGNL1 hexamer assembly.

24 Jan 2025·Science

Molecular basis of FIGNL1 in dissociating RAD51 from DNA and chromatin

Article

Author: Wang, Raymond ; Yu, Tai-Yuan ; Jasin, Maria ; Carver, Alexander ; White, Travis ; Zhang, Xiaodong ; Yates, Luke A. ; Lister, Katie

Maintaining genome integrity is an essential and challenging process. RAD51 recombinase, the central component of several crucial processes in repairing DNA and protecting genome integrity, forms filaments on DNA, which are tightly regulated. One of these RAD51 regulators is FIGNL1 (fidgetin-like 1), which prevents RAD51 genotoxic chromatin association in normal cells and persistent RAD51 foci upon DNA damage. The cryogenic electron microscopy–imaged structure of FIGNL1 in complex with RAD51 reveals that FIGNL1 forms a nonplanar hexamer and encloses RAD51 N terminus in the FIGNL1 hexamer pore. Mutations in pore loop or catalytic residues of FIGNL1 render it defective in filament disassembly and are lethal in mouse embryonic stem cells. Our study reveals a distinct mechanism for removing RAD51 from bound substrates and provides the molecular basis for FIGNL1 in maintaining genome stability.

01 Jan 2025·Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

Evolution and functional divergence of the Fidgetin family

Review

Author: Yan, Yingying ; Wang, Qing ; Qiang, Liang Oscar ; Liu, Mei ; Dong, Zhangji

The Fidgetin (FIGN) family, which comprises FIGN, Fidgetin-like 1 (FIGNL1), and Fidgetin-like 2 (FIGNL2), is a vital group of microtubule-severing proteins. These proteins feature a conserved AAA+ domain essential for ATPase activity and a hexameric assembly. This review provides an in-depth analysis of the evolution and functional divergence of the FIGN family members, highlighting their role in the dynamic organization of the cytoskeleton. We further explore their broader biological functions across various species, systems, and subcellular localization. Although the FIGN family is conserved, each member exhibits unique structural characteristics and functions that reflect their evolutionary adaptations. FIGNL1 is found across animal species, while FIGNL2 is specific to vertebrates, thereby indicating its more recent evolutionary origin. Moreover, synteny analysis has revealed that FIGN is located in a more conserved genomic region compared to FIGNL2, which has undergone substantial evolutionary changes. The expression patterns of the FIGN members also vary across organisms and tissues. For example, FIGNL2 shows a notably reduced expression in the mammalian nervous system compared to that in lower vertebrates. The FIGN family members have distinct roles in microtubule severing, cell division, and DNA repair. Specifically, FIGN is involved in cell division and neuronal regeneration, FIGNL1 in axonal growth and DNA repair, and FIGNL2 in cell migration and vascular development. Their involvement in these processes underscores their role as potential biomarkers for certain cancers as well as therapeutic targets for diseases affecting the nervous system and cardiovascular development. All these evolutionary insights and functional distinctions of the FIGN family offer a comprehensive framework for understanding cytoskeletal regulation and its implications in health and disease.

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FIGNL1

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