Ample evidence exists that ADNP is of key importance for proper functioning of the nBAF complex. This functional relation between ADNP and the nBAF complex is mediated by direct protein-protein interaction of ADNP with several of the BAF subunits [Mandel and Gozes, 2007]. ADNP directly binds to SMARCA2, SMARCA4, and SMARCC2, through its C-terminal end (Fig. 4). Furthermore, reciprocal interactions have been demonstrated between ADNP, the heterochromatin-enriched protein HP1α, and BAF complexes. ADNP is recruited to the pericentromeric heterochromatin through binding of the P*V*L and ARKs motif to HP1α. It can be hypothesized that ADNP by its zinc fingers and homeobox domain functions as an anchoring protein that binds to specific positions in the DNA to guide the protein remodeling complex to its target regions. This way, dysfunction of ADNP results in deregulation of BAF-mediated chromatin remodeling.
