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The Fanconi anaemia (FA) nuclear complex (composed of the FA proteins A, C, G and F) is essential for protection against chromosome breakage. It activates the downstream protein FANCD2 by monoubiquitylation; this then forges an association with the BRCA1 protein at sites of DNA damage. Here we show that the recently identified FANCE protein is part of this nuclear complex, binding both FANCC and FANCD2. Indeed, FANCE is required for the nuclear accumulation of FANCC and provides a critical bridge between the FA complex and FANCD2. Disease-associated FANCC mutants do not bind to FANCE, cannot accumulate in the nucleus and are unable to prevent chromosome breakage.

Original publication

DOI

10.1093/emboj/cdf355

Type

Journal article

Journal

EMBO J

Publication Date

01/07/2002

Volume

21

Pages

3414 - 3423

Keywords

Active Transport, Cell Nucleus, Amino Acid Substitution, Animals, Bacterial Proteins, COS Cells, Cell Cycle Proteins, Cell Line, Cell Nucleus, Chlorocebus aethiops, Chromosome Breakage, DNA-Binding Proteins, Fanconi Anemia, Fanconi Anemia Complementation Group C Protein, Fanconi Anemia Complementation Group D2 Protein, Fanconi Anemia Complementation Group E Protein, Fanconi Anemia Complementation Group F Protein, Fanconi Anemia Complementation Group G Protein, Fanconi Anemia Complementation Group Proteins, HeLa Cells, Humans, Luminescent Proteins, Macromolecular Substances, Mutation, Missense, Nuclear Proteins, Protein Binding, Protein Interaction Mapping, Proteins, RNA-Binding Proteins, Recombinant Fusion Proteins, Structure-Activity Relationship