ArticleNucleic acids research1998
Mapping of interaction domains between human repair proteins ERCC1 and XPF.
Article in Nucleic acids research, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 119 citations in OpenAlex.
- Rad1-Rad10 uses different interfaces to interact with pathway-specific DNA repair factors.Nucleic acids research · 2026Article
- A new multisystem ERCC1-hepatorenal syndrome: insights from a clinical cohort, molecular pathogenesis, and management guidelines.European journal of human genetics : EJHG · 2025Article
- CARM1/PRMT4 facilitates XPF-ERCC1 heterodimer assembly and maintains nucleotide excision repair activity.Nucleic acids research · 2025Article
- Calorie restriction increases the sensitivity of progeroid Ercc1GeroScience · 2025Article
- A complex phylogeny of lineage plasticity in metastatic castration resistant prostate cancer.NPJ precision oncology · 2025Article
- Critical role of alpha spectrin in DNA repair: the importance of μ-calpain and Fanconi anemia proteins.Experimental biology and medicine (Maywood, N.J.) · 2025Review
- Noise Stress Abrogates Structure-Specific Endonucleases within the Mammalian Inner Ear.International journal of molecular sciences · 2024Article
- A novel algorithm for the virtual screening of extensive small molecule libraries against ERCC1/XPF protein-protein interaction for the identification of resistance-bypassing potential anticancer molecules.Turkish journal of biology = Turk biyoloji dergisi · 2024Article
- Mechanism of action of nucleotide excision repair machinery.Biochemical Society transactions · 2022Review
- Every protagonist has a sidekick: Structural aspects of human xeroderma pigmentosum-binding proteins in nucleotide excision repair.Protein science : a publication of the Protein Society · 2021Review
- ERCC1 mutations impede DNA damage repair and cause liver and kidney dysfunction in patients.The Journal of experimental medicine · 2021Article
- Clinical Perspectives of ERCC1 in Bladder Cancer.International journal of molecular sciences · 2020Review
- Acetylation of XPF by TIP60 facilitates XPF-ERCC1 complex assembly and activation.Nature communications · 2020Article
- Fanconi anemia pathway as a prospective target for cancer intervention.Cell & bioscience · 2020Review
- The functional importance of lamins, actin, myosin, spectrin and the LINC complex in DNA repair.Experimental biology and medicine (Maywood, N.J.) · 2019Review
- DCAF7 is required for maintaining the cellular levels of ERCC1-XPF and nucleotide excision repair.Biochemical and biophysical research communications · 2019Article
- Deficiency of nucleotide excision repair is associated with mutational signature observed in cancer.Genome research · 2019Article
- Function and Interactions of ERCC1-XPF in DNA Damage Response.Molecules (Basel, Switzerland) · 2018Review
- Spectrin and its interacting partners in nuclear structure and function.Experimental biology and medicine (Maywood, N.J.) · 2018Review
- ERCC4 variants identified in a cohort of patients with segmental progeroid syndromes.Human mutation · 2018Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ERCC1-XPF is a heterodimeric protein complexinvolved in nucleotide excision repair and recombinational processes. Like its homologous complex in Saccharomyces cerevisiae , Rad10-Rad1, it acts as a structure-specific DNA endonuclease, cleaving at duplex-single-stranded DNA junctions. In repair, ERCC1-XPF and Rad10-Rad1 make an incision on the the 5'-side of the lesion. No humans with a defect in the ERCC1 subunit of this protein complex have been identified and ERCC1-deficient mice suffer from severe developmental problems and signs of premature aging on top of a repair-deficient phenotype. Xeroderma pigmentosum group F patients carry mutations in the XPF subunit and generally show the clinical symptoms of mild DNA repair deficiency. All XP-F patients examined demonstrate reduced levels of XPF and ERCC1 protein, suggesting that proper complex formation is required for stability of the two proteins. To better understand the molecular and clinical consequences of mutations in the ERCC1-XPF complex, we decided to map the interaction domains between the two subunits. The XPF-binding domain comprises C-terminal residues 224-297 of ERCC1. Intriguingly, this domain resides outside the region of homology with its yeast Rad10 counterpart. The ERCC1-binding domain in XPF maps to C-terminal residues 814-905. ERCC1-XPF complex formation is established by a direct interaction between these two binding domains. A mutation from an XP-F patient that alters the ERCC1-binding domain in XPF indeed affects complex formation with ERCC1.
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