Fig. 2.
Fig. 2. Fusion proteins in acute promyelocytic leukemia. (A) indicates the unliganded interactions of the RXR/RAR heterodimer with an N-CoR/Sin3/HDAC1 complex. Upon binding retinoid acid, the RXR/RAR heterodimer releases the corepressor complex and binds a coactivator complex with histone acetylase activity. (B) indicates the analogous interactions of the RXR/PML-RAR heterodimer with the corepressor complex. Release of the corepressor complex occurs only in the presence of pharmacological levels of retinoic acid. (C) depicts the ligand-independent binding of the corepressor complex to PLZF-RAR. (It has been proposed, but not yet been formally demonstrated, that liganded RXR/PLZF-RAR binds both coactivator and corepressor complexes.) Chromatin remodeling occurs only in the presence of both RA and an HDAC inhibitor.

Fusion proteins in acute promyelocytic leukemia. (A) indicates the unliganded interactions of the RXR/RAR heterodimer with an N-CoR/Sin3/HDAC1 complex. Upon binding retinoid acid, the RXR/RAR heterodimer releases the corepressor complex and binds a coactivator complex with histone acetylase activity. (B) indicates the analogous interactions of the RXR/PML-RAR heterodimer with the corepressor complex. Release of the corepressor complex occurs only in the presence of pharmacological levels of retinoic acid. (C) depicts the ligand-independent binding of the corepressor complex to PLZF-RAR. (It has been proposed, but not yet been formally demonstrated, that liganded RXR/PLZF-RAR binds both coactivator and corepressor complexes.) Chromatin remodeling occurs only in the presence of both RA and an HDAC inhibitor.

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