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FANCM-FAAP24 and FANCJ: FA proteins that metabolize DNA Ali AM; Singh TR; Meetei ARMutat Res 2009[Jul]; 668 (1-2): 20-6Fanconi anemia (FA) is a rare autosomal recessive or X-linked disorder characterized by aplastic anemia, cancer susceptibility and cellular sensitivity to DNA-crosslinking agents. Eight FA proteins (FANCA, -B, -C, -E, -F, -G, -L and -M) and three non-FA proteins (FAAP100, FAAP24 and HES1) form the FA nuclear core complex that is required for monoubiquitination of the FANCD2-FANCI dimer upon DNA damage. The other three FA proteins, FANCD1/BRCA2, FANCJ/BACH1/BRIP1 and FANCN/PALB2, act in parallel or downstream of the FANCD2-FANCI dimer. Despite the isolation and characterization of several FA proteins, the mechanism by which these proteins protect cells from DNA interstrand crosslinking agents has been unclear. This is because a majority of the FA proteins lack any recognizable functional domains that can provide insight into their function. The recently discovered FANCM (Hef) and FANCJ (BRIP1/BACH1) proteins contain helicase domains, providing potential insight into the role of FA proteins in DNA repair. FANCM with its partner, FAAP24, and FANCJ bind and metabolize a variety of DNA substrates. In this review, we focus on the discovery, structure, and function of the FANCM-FAAP24 and FANCJ proteins.|*DNA Repair[MESH]|Basic-Leucine Zipper Transcription Factors/chemistry/*metabolism[MESH]|DNA Helicases/chemistry/*metabolism[MESH]|DNA-Binding Proteins/chemistry/*metabolism[MESH]|DNA/metabolism[MESH]|Drug Discovery[MESH]|Fanconi Anemia Complementation Group Proteins/chemistry/*metabolism[MESH]|Fanconi Anemia/*metabolism[MESH]|Humans[MESH]|Structure-Activity Relationship[MESH] |
