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Fig. 4. The N terminus of D-mib mediates physical association with both Delta and Serrate. Co-immunoprecipitation was performed on lysates from 293T cells transfected with polyoma-tagged DSL ligands and Myc-tagged D-mib proteins. Structures of D-mib variants are depicted in Fig. 1. In transfected cells, D-mib proteins appear as single bands (A, lanes 6-10), Delta is present in full-length form and as a cleavage product corresponding to its intracellular domain (B, lanes 16-20), and Serrate appears as a series of relatively closely migrating bands (C, lanes 26-30). (A) Delta efficiently co-immunoprecipitates D-mib-N, D-mib ${Delta}$ 3RF and D-mib ${Delta}$ RF (lanes 2-4). (B) Delta is efficiently co-immunoprecipitated by D-mib-N, D-mib ${Delta}$ 3RF and D-mib ${Delta}$ RF (lanes 12-14); D-mib-N also associates with the cleaved intracellular domain of Delta (lane 12). Full-length D-mib interacts weakly with Delta (lane 11), but levels of Delta are also decreased in the presence of D-mib (lane 16). (C) Serrate is co-immunoprecipitated by D-mib-N, D-mib ${Delta}$ 3RF and D-mib ${Delta}$ RF (lanes 22-24), and D-mib reduces overall levels of Serrate (lane 26). In all cases, the interaction between DSL ligands and D-mib-N is strongest.

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