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Showing FIRRMC1ORF112 is a alias.

FIRRM

FIGNL1-interacting regulator of recombination and mitosis · UniProt Q9NSG2

Length
853 aa
Mass
96.6 kDa
Annotated
2026-06-09
17 papers in source corpus 10 papers cited in narrative 10 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 5/5 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

FIRRM (C1orf112/FLIP/Apolo1) is a genome-stability factor that, through a stable complex with the AAA+ ATPase FIGNL1, controls the dynamics of RAD51 (and the meiotic recombinase DMC1) on chromatin to ensure faithful homologous recombination (PMID:37347663, PMID:38286805, PMID:37515771). FIRRM and FIGNL1 are mutually stabilizing partners, and FIRRM directly stimulates the RAD51 filament-disassembly activity of FIGNL1, limiting RAD51 accumulation both with and without exogenous damage and promoting RAD51 dissociation from nucleofilaments after strand invasion to complete recombination (PMID:38286805, PMID:37515771); this disassembly activity has been reconstituted in vitro with purified proteins, where BRCA2 acts upstream to protect filaments from premature disassembly by the complex (PMID:37515771, PMID:38133958). Loss of FIRRM produces ultrafine DNA bridges, persistent RAD51 foci, defective replication fork progression, hypersensitivity to interstrand crosslinking agents with S-G2 damage accumulation and chromosomal aberrations, the complex acting at ICLs in part by controlling MUS81 chromatin loading (PMID:37347663, PMID:37256941, PMID:38286805). The FIGNL1-FIRRM complex is likewise essential for meiotic recombination, limiting RAD51/DMC1 loading on intact chromatin independently of SPO11-generated breaks and altering recombinase filament structure to inhibit strand invasion in vitro, with mouse knockouts causing meiotic prophase arrest and early embryonic lethality (PMID:37256941, PMID:39147779). Independently of its recombination role, FIRRM localizes to kinetochores in prometaphase where it serves as a PLK1 substrate, bridging PLK1 and PP1γ in a feedback loop that tunes PLK1 activity for accurate kinetochore-microtubule attachment and chromosome segregation (PMID:34260926).

Mechanistic history

Synthesis pass · year-by-year structured walk · 9 steps
  1. 2021 High

    Established a mitotic role for FIRRM distinct from any recombination function by placing it at kinetochores as a regulator of PLK1 activity.

    Evidence FRET-based PLK1 activity reporter, live-cell kinetochore imaging, kinase substrate and PP1γ dephosphorylation assays, siRNA with chromosome alignment phenotype

    PMID:34260926

    Open questions at the time
    • Relationship between the kinetochore/PLK1 role and the FIGNL1/RAD51 role is unresolved
    • Structural basis of PLK1-FIRRM-PP1γ bridging not defined
  2. 2023 High

    Identified FIRRM as a stabilizing partner of the AAA+ ATPase FIGNL1 that regulates RAD51 dynamics at replication forks, explaining UFB formation and fork defects on its loss.

    Evidence Genome-wide loss-of-function screen, Co-IP, RAD51 foci analysis, replication fork dynamics and UFB imaging

    PMID:37347663

    Open questions at the time
    • Direct enzymatic mechanism not yet reconstituted at this stage
    • Did not define FIRRM action at ICLs versus other lesions
  3. 2023 High

    Defined FIRRM's role in interstrand crosslink repair, linking it to MUS81 chromatin loading, HR-intermediate resolution, and a HR-deficiency mutational signature, with in vivo essentiality.

    Evidence CRISPR screens, ICL sensitivity and cell-cycle assays, chromatin fractionation for MUS81, laser-induced ICL recruitment, chromosomal aberration analysis, mouse knockout

    PMID:37256941

    Open questions at the time
    • How FIRRM controls MUS81 loading mechanistically is not defined
    • Whether ICL role is fully FIGNL1-dependent not resolved here
  4. 2023 High

    Dissected the FIRRM-FIGNL1 interdependence and revealed a potential FIGNL1-independent FIRRM activity, plus direct ssDNA binding.

    Evidence CRISPR screen, Co-IP for complex stability, ΔWCF domain-deletion mutagenesis, RAD51 foci analysis, in vitro ssDNA binding assay

    PMID:37556550

    Open questions at the time
    • Functional significance of ssDNA binding not established
    • Nature of the FIGNL1-independent function not defined
  5. 2023 High

    Provided the biochemical mechanism: FIRRM directly stimulates FIGNL1-mediated RAD51 filament disassembly, with BRCA2 acting upstream to protect filaments.

    Evidence RAD51 proximity proteomics, Co-IP, in vitro RAD51 filament disassembly reconstitution with purified proteins, epistasis analysis

    PMID:37515771 PMID:38133958

    Open questions at the time
    • Stoichiometry and structure of the complex on filaments unknown
    • How BRCA2 antagonism is regulated in cells not defined
  6. 2024 High

    Consolidated the stable FIRRM-FIGNL1 complex as the unit limiting chromatin RAD51 and promoting filament dissociation to complete HR and maintain fork progression.

    Evidence Co-IP, RAD51 chromatin fractionation/foci quantification, DNA fiber assay, HR reporter, ICL sensitivity, epistasis

    PMID:38286805

    Open questions at the time
    • Temporal coordination of disassembly during HR steps not mapped
    • Regulation of the complex by post-translational signals unknown
  7. 2024 High

    Extended the complex's function to meiosis, showing it limits RAD51/DMC1 loading independently of SPO11 breaks and directly alters recombinase filament structure to inhibit strand invasion.

    Evidence Germline-specific conditional knockout mice, RAD51/DMC1 immunofluorescence, in vitro strand invasion assay with purified FIGNL1ΔN, filament structure analysis

    PMID:39147779

    Open questions at the time
    • Specific FIRRM contribution within the meiotic complex not separately reconstituted
    • How DMC1 versus RAD51 selectivity is achieved unknown
  8. 2024 Medium

    Linked FIRRM expression to mitochondrial function under methionine restriction in cancer cells, a context distinct from its recombination role.

    Evidence Transcriptomics, knockdown in osteosarcoma cells, mitochondrial function assays, xenografts

    PMID:38769167

    Open questions at the time
    • Link to mitochondrial function is correlative/knockdown-based without direct biochemical mechanism
    • Connection to RAD51 or PLK1 roles unclear
  9. 2026 Medium

    Connected FIRRM to mitotic entry in hepatocellular carcinoma via PLK1 phosphorylation, reinforcing the PLK1 axis in a tumor context.

    Evidence CRISPR knockout in HCC cell lines, PLK1 phosphorylation western blot, flow-cytometry cell-cycle analysis, in vivo tumor proliferation

    PMID:42007975

    Open questions at the time
    • No mechanistic dissection beyond PLK1 phosphorylation level
    • Single-lab observation; relationship to kinetochore feedback loop not addressed

Open questions

Synthesis pass · forward-looking unresolved questions
  • How FIRRM's two roles — FIGNL1-dependent RAD51 disassembly and PLK1/PP1γ mitotic regulation — are integrated or temporally separated within the cell remains unresolved.
  • No structural model of FIRRM or its complexes
  • Whether the FIGNL1-independent and PLK1 roles share a domain is unknown
  • Regulatory cues switching between functions undefined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0098772 molecular function regulator activity 2 GO:0003677 DNA binding 1 GO:0003723 RNA binding 1
Localization
GO:0005634 nucleus 2 GO:0000228 nuclear chromosome 1
Pathway
R-HSA-73894 DNA Repair 3 R-HSA-1640170 Cell Cycle 2 R-HSA-1474165 Reproduction 1
Complex memberships
FIGNL1-FIRRM complex

Evidence

Reading pass · 10 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2023 FIRRM interacts with and stabilizes the AAA+ ATPase FIGNL1; inactivation of either FIRRM or FIGNL1 results in ultrafine DNA bridge (UFB) formation, prolonged accumulation of RAD51 at nuclear foci, and impaired replication fork dynamics, indicating that FIRRM-FIGNL1 regulates RAD51 dynamics at replication forks to maintain genome integrity. Genome-wide loss-of-function screen, co-immunoprecipitation, RAD51 foci analysis, replication fork dynamics assay, UFB imaging Cell reports High 37347663
2021 Apolo1 (FIRRM) localizes to kinetochores during early mitosis, sustains PLK1 kinase activity at kinetochores during prometaphase for accurate kinetochore-microtubule attachment, is a cognate substrate of PLK1 (phosphorylated by PLK1), and phosphorylation enables PP1γ to subsequently inactivate PLK1 by dephosphorylation — constituting a feedback loop that governs PLK1 activity. FRET-based PLK1 activity reporter, live-cell imaging (kinetochore localization), kinase substrate assay, phosphatase (PP1γ) interaction/dephosphorylation assay, siRNA knockdown with chromosome alignment phenotype Cell reports High 34260926
2023 FIRRM is recruited to ICL (interstrand crosslink) sites, controls MUS81 chromatin loading, and thereby mediates resolution of homologous recombination intermediates generated during ICL repair; FIRRM deficiency causes hypersensitivity to ICL agents, DNA damage accumulation in S-G2, chromosomal aberrations, and a unique mutational signature associated with HR deficiency. Complementary CRISPR genetic screens, ICL sensitivity assays, cell cycle analysis (DNA damage accumulation in S-G2), chromatin fractionation (MUS81 loading), recruitment to ICLs (laser-induced damage foci), chromosomal aberration analysis, mouse knockout (early embryonic lethality) Science advances High 37256941
2024 FIRRM (FLIP/C1orf112) forms a stable complex with FIGNL1 that is required to limit RAD51 amounts and foci on chromatin both in the presence and absence of exogenous DNA damage, and to promote RAD51 dissociation from nucleofilaments to complete HR; FLIP loss causes defective replication fork progression and reduced HR competency. Co-immunoprecipitation (stable complex), RAD51 chromatin fractionation/foci quantification, replication fork progression assay (fiber assay), HR reporter assay, ICL sensitivity assay, epistasis analysis Nature communications High 38286805
2024 The FIGNL1-FIRRM complex is essential for meiotic recombination; both proteins are required for completing meiotic prophase in mouse spermatocytes, and the complex limits RAD51 and DMC1 accumulation on intact chromatin independently of SPO11-catalyzed DSBs. Purified human FIGNL1ΔN alters the RAD51/DMC1 nucleoprotein filament structure and inhibits strand invasion in vitro. Male germline-specific conditional knockout (cKO) mouse models, immunofluorescence (RAD51/DMC1 foci), in vitro strand invasion assay with purified proteins, nucleoprotein filament structure analysis Nature communications High 39147779
2023 FIRRM cooperates with FIGNL1 to promote resolution of RAD51 foci at ICL-induced DSBs; FIRRM stability is interdependent with FIGNL1. A FIRRM mutant lacking the WCF domain (ΔWCF) stabilizes FIRRM independently of FIGNL1 and rescues RAD51 foci resolution and cell survival, suggesting FIGNL1-independent function. FIRRM also binds preferentially to single-stranded DNA in vitro. CRISPR screen, Co-immunoprecipitation (FIRRM-FIGNL1 complex/stability), RAD51 foci analysis, domain-deletion mutagenesis (ΔWCF), in vitro ssDNA binding assay Science advances High 37556550
2023 C1orf112 (FIRRM) physically interacts with FIGNL1, enhances FIGNL1 protein stability, and directly stimulates the RAD51 filament disassembly activity of FIGNL1. BRCA2 directly interacts with the C1orf112-FIGNL1 complex and functions upstream to protect RAD51 filaments from premature disassembly by this complex. RAD51 proximity proteomics, Co-immunoprecipitation, in vitro RAD51 filament disassembly assay with purified proteins, protein stability assay, epistasis analysis (BRCA2 upstream) Cell reports High 37515771
2023 The in vitro reconstitution of RAD51 filament disassembly by purified C1orf112/FIRRM-FIGNL1 complex was validated, and the antagonistic effect between C1orf112/FIRRM-FIGNL1 and BRCA2 on RAD51 filament stabilization was demonstrated biochemically using purified proteins from E. coli or S. cerevisiae. Protein purification from E. coli and S. cerevisiae, in vitro RAD51 filament disassembly reconstitution, competition assay with purified miBRCA2 STAR protocols High 38133958
2026 FIRRM knockout in hepatocellular carcinoma cells reduces PLK1 phosphorylation and inhibits mitotic progression and the G2-to-M transition of the cell cycle, establishing that FIRRM promotes mitotic entry via PLK1-mediated signaling. CRISPR knockout of FIRRM in HCC cell lines, PLK1 phosphorylation assay (western blot), cell cycle analysis (flow cytometry), in vivo tumor proliferation assay Journal of gastroenterology Medium 42007975
2024 Methionine restriction reduces C1orf112 expression in osteosarcoma cells, and reduced C1orf112 expression underlies methionine deprivation-initiated suppression of mitochondrial functions (dysregulated respiratory chain gene expression, increased mitochondrial ROS, reduced ATP production, decreased respiration, damaged mitochondrial membrane potential). Transcriptomic analysis, C1orf112 expression knockdown in cultured cells, mitochondrial function assays (ROS, ATP, oxygen consumption, membrane potential), xenograft models Cell death & disease Medium 38769167

Source papers

Stage 0 corpus · 17 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2023 FIRRM/C1orf112 is synthetic lethal with PICH and mediates RAD51 dynamics. Cell reports 24 37347663
2021 Feedback control of PLK1 by Apolo1 ensures accurate chromosome segregation. Cell reports 24 34260926
2024 Deprivation of methionine inhibits osteosarcoma growth and metastasis via C1orf112-mediated regulation of mitochondrial functions. Cell death & disease 21 38769167
2021 Pan-Cancer Analysis Identified C1ORF112 as a Potential Biomarker for Multiple Tumor Types. Frontiers in molecular biosciences 21 34490347
2021 Evolution, structure and emerging roles of C1ORF112 in DNA replication, DNA damage responses, and cancer. Cellular and molecular life sciences : CMLS 17 33625522
2023 FIRRM/C1orf112 mediates resolution of homologous recombination intermediates in response to DNA interstrand crosslinks. Science advances 16 37256941
2024 FLIP(C1orf112)-FIGNL1 complex regulates RAD51 chromatin association to promote viability after replication stress. Nature communications 12 38286805
2024 FIGNL1-FIRRM is essential for meiotic recombination and prevents DNA damage-independent RAD51 and DMC1 loading. Nature communications 11 39147779
2023 C1orf112 teams up with FIGNL1 to facilitate RAD51 filament disassembly and DNA interstrand cross-link repair. Cell reports 10 37515771
2023 FIRRM cooperates with FIGNL1 to promote RAD51 disassembly during DNA repair. Science advances 10 37556550
2021 High Expression of C1ORF112 Predicts a Poor Outcome: A Potential Target for the Treatment of Low-Grade Gliomas. Frontiers in genetics 8 34880897
2024 FIRRM and FIGNL1: partners in the regulation of homologous recombination. Trends in genetics : TIG 7 38494375
2026 C1orf112 promotes breast cancer growth by modulating the cell cycle. Frontiers in bioengineering and biotechnology 0 41878691
2026 Novel driver gene FIRRM regulates the cell cycle for promoting tumor growth in hepatocellular carcinoma. Journal of gastroenterology 0 42007975
2025 Molecular mechanisms by which C1orf112 promotes endometrial cancer progression and the development and validation of a clinical scoring model. Clinical epigenetics 0 41239389
2023 RADIF(C1orf112)-FIGNL1 Complex Regulates RAD51 Chromatin Association to Promote Viability After Replication Stress. bioRxiv : the preprint server for biology 0 37808755
2023 Reconstitution of the antagonistic effect between C1orf112/FIRRM-FIGNL1 and BRCA2 on RAD51 filament stabilization. STAR protocols 0 38133958

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