Characterization of a novel protein-protein interaction between DLX proteins and a member of the BTB/POZ family
The mammalian 'Distal-less homeobox (Dlx)' gene family is composed of six paralogues, which play important roles in patterning and differentiation of a variety of embryonic tissues. 'Dlx' genes are expressed in the developing axial and appendicular skeleton, branchial arches, forebrain and placenta. The DNA binding specificity of homeodomain proteins is often not sufficient to account for their specific developmental functions, suggesting that biological specificity is in part conferred by protein-protein interactions. Previously, we identified a member of the BTB/POZ domain family as a Dlx6 binding partner in a yeast two-hybrid screen. Here we map the interaction domains using a GST pulldown assay and further confirmed the interaction by co-immunopreciptation. Additionally, the two proteins co-localized in the nuclei of co-transfected HEK-293T cells.