Figure 6.
Figure 6. A model for the architecture of the nuclear FA protein complex. Letters indicate the FANC proteins investigated in this study. FANCG can directly bind to both FANCA and FANCF as well as mediate an interaction between them. The FANCG-mediated multimerization of FANCA is presented in one of the simpler possible forms. This study demonstrated direct interaction of FANCC only with FANCE, although previous immunoprecipitation experiments have suggested that both FANCC and FANCE are part of the nuclear FA complex (dotted lines). FANCE is currently the only FANC protein demonstrated to interact either directly or indirectly with FANCD2. Thus, in the absence of evidence otherwise, FANCE is shown as exiting the core FA complex to bind to FANCD2. With the exception of the FANCG-mediated FANCA multimerization demonstrated in this study, all interactions among the FANC proteins are presented as occurring with 1:1 stoichiometry for simplicity.

A model for the architecture of the nuclear FA protein complex. Letters indicate the FANC proteins investigated in this study. FANCG can directly bind to both FANCA and FANCF as well as mediate an interaction between them. The FANCG-mediated multimerization of FANCA is presented in one of the simpler possible forms. This study demonstrated direct interaction of FANCC only with FANCE, although previous immunoprecipitation experiments have suggested that both FANCC and FANCE are part of the nuclear FA complex (dotted lines). FANCE is currently the only FANC protein demonstrated to interact either directly or indirectly with FANCD2. Thus, in the absence of evidence otherwise, FANCE is shown as exiting the core FA complex to bind to FANCD2. With the exception of the FANCG-mediated FANCA multimerization demonstrated in this study, all interactions among the FANC proteins are presented as occurring with 1:1 stoichiometry for simplicity.

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