FIGNL1-interacting regulator of recombination and mitosis (FIRRM)

FIGNL1-interacting regulator of recombination and mitosis (FIRRM) is a protein that forms a complex with Fidgetin-like 1 (FIGNL1) and regulates homologous recombination (HR) through the control of RAD51 and DMC1 nucleoprotein filament dynamics during both meiosis and DNA interstrand crosslink (ICL) repair[1][2][3]. FIRRM acts as a scaffold, stabilizing FIGNL1 and enabling proper disassembly of RAD51 filaments from single-stranded DNA at sites of DNA double-strand breaks, thereby facilitating effective repair and chromosome segregation[1][3]. FIRRM is required for proper meiotic progression and genomic stability; loss of FIRRM leads to defective repair of meiotic double-strand breaks and failure of synapsis, with consequences for cell viability[1][2]. FIRRM has independent as well as FIGNL1-dependent functions and may have additional roles in mitosis and cancer, where it is emerging as a potential biomarker for prognosis, particularly in aggressive tumor subtypes[3].

Other names

C1orf112APOLO1FLIPFLJ10706MEICA1POLO1-associating proteinFidgetin-like-1 interacting proteinApolo1

Not applicable (no drugs/ligands currently known to directly target FIRRM; modulation of RAD51 dynamics via FIRRM-FIGNL1 complex is a mechanistic function)