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Identification of FAAP24, a Fanconi Anemia Core Complex Protein that Interacts with FANCM
- Source :
- Molecular Cell. 25:331-343
- Publication Year :
- 2007
- Publisher :
- Elsevier BV, 2007.
-
Abstract
- The Fanconi anemia (FA) core complex plays a crucial role in a DNA damage response network with BRCA1 and BRCA2. How this complex interacts with damaged DNA is unknown, as only the FA core protein FANCM (the homolog of an archaeal helicase/nuclease known as HEF) exhibits DNA binding activity. Here, we describe the identification of FAAP24, a protein that targets FANCM to structures that mimic intermediates formed during the replication/repair of damaged DNA. FAAP24 shares homology with the XPF family of flap/fork endonucleases, associates with the C-terminal region of FANCM, and is a component of the FA core complex. FAAP24 is required for normal levels of FANCD2 monoubiquitylation following DNA damage. Depletion of FAAP24 by siRNA results in cellular hypersensitivity to DNA crosslinking agents and chromosomal instability. Our data indicate that the FANCM/FAAP24 complex may play a key role in recruitment of the FA core complex to damaged DNA.
- Subjects :
- DNA Replication
congenital, hereditary, and neonatal diseases and abnormalities
Fanconi anemia, complementation group C
DNA Repair
DNA damage
Molecular Sequence Data
chemistry.chemical_compound
Fanconi anemia
Two-Hybrid System Techniques
hemic and lymphatic diseases
FANCD2
medicine
Humans
Amino Acid Sequence
FANCM
Molecular Biology
Sequence Homology, Amino Acid
biology
Ubiquitin
FAN1
DNA Helicases
nutritional and metabolic diseases
Helicase
Cell Biology
medicine.disease
Molecular biology
Fanconi Anemia Complementation Group Proteins
Protein Structure, Tertiary
DNA-Binding Proteins
chemistry
Multigene Family
biology.protein
Sequence Alignment
DNA
DNA Damage
Subjects
Details
- ISSN :
- 10972765
- Volume :
- 25
- Database :
- OpenAIRE
- Journal :
- Molecular Cell
- Accession number :
- edsair.doi.dedup.....a68ec4ff32d8ba7ce0c365e79cba20aa
- Full Text :
- https://doi.org/10.1016/j.molcel.2007.01.003