The Fanconi anemia protein interaction network: Casting a wide net
| Autor: | Meghan A. Rego, Niall G. Howlett, Fred W. Kolling |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Fanconi anemia
complementation group C DNA Repair DNA damage DNA repair Health Toxicology and Mutagenesis Diepoxybutane Biology Models Biological Article chemistry.chemical_compound Fanconi anemia Chromosomal Instability Chromosome instability Genetics medicine Humans Molecular Biology Recombination Genetic Epistasis Genetic DNA medicine.disease Molecular biology Fanconi Anemia Complementation Group Proteins Fanconi Anemia chemistry Homologous recombination |
| Zdroj: | Mutation Research/Fundamental and Molecular Mechanisms of Mutagenesis. 668:27-41 |
| ISSN: | 0027-5107 |
| DOI: | 10.1016/j.mrfmmm.2008.11.018 |
| Popis: | It has long been hypothesized that a defect in the repair of damaged DNA is central to the etiology of Fanconi anemia (FA). Indeed, an increased sensitivity of FA patient-derived cells to the lethal effects of various forms of DNA damaging agents was described over three decades ago [A.J. Fornace, Jr., J.B. Little, R.R. Weichselbaum, DNA repair in a Fanconi's anemia fibroblast cell strain, Biochim. Biophys. Acta 561 (1979) 99-109; Y. Fujiwara, M. Tatsumi, Repair of mitomycin C damage to DNA in mammalian cells and its impairment in Fanconi's anemia cells, Biochem. Biophys. Res. Commun. 66 (1975) 592-598; A.J. Rainbow, M. Howes, Defective repair of ultraviolet- and gamma-ray-damaged DNA in Fanconi's anaemia, Int. J. Radiat. Biol. Relat. Stud. Phys. Chem. Med. 31 (1977) 191-195]. Furthermore, the cytological hallmark of FA, the DNA crosslink-induced radial chromosome formation, exemplifies an innate impairment in the repair of these particularly cytotoxic DNA lesions [A.D. Auerbach, Fanconi anemia diagnosis and the diepoxybutane (DEB) test, Exp. Hematol. 21 (1993) 731-733]. Precisely defining the collective role of the FA proteins in DNA repair, however, continues to be one of the most enigmatic and challenging questions in the FA field. The first six identified FA proteins (A, C, E, F, G, and D2) harbored no recognizable enzymatic features, precluding association with a specific metabolic process. Consequently, our knowledge of the role of the FA proteins in the DNA damage response has been gleaned primarily through biochemical association studies with non-FA proteins. Here, we provide a chronological discourse of the major FA protein interaction network discoveries, with particular emphasis on the DNA damage response, that have defined our current understanding of the molecular basis of FA. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect