Daxx is essential for embryonic development and implicated in apoptosis and transcriptional regulation. It is found only in the animal kingdom and appears to arise first in insects. In the Drosophila genus, the Daxx orthologs are much larger than those in other species. Here we show that in addition to a conserved core of ~200 residues, Daxx possesses several conserved domains and two essentially invariable short SUMO-interacting motifs (SIMs), each located at one or the other terminus of the protein.
p53 SUMOylation promotes its nuclear export. The SIM-binding groove of a SUMO moiety linked to p53 and a SIM in CRM1 regulates their interaction. CRM1 binds to tetrameric p53 with a properly folded core domain, and CRM1 with a mutated SIM in the HEAT9 loop accumulates with SUMOylated p53 at NPCs and cytoplasmic aggregates.
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