Fig. 4. dVps16 proteins bind to Dor. The binding of different dVps16A truncations (outlined in panel E) to Dor was evaluated by co-immunoprecipitation experiments. (A) Myc-tagged full-length or truncated dVps16A proteins were co-expressed with Myc-Dor and detected with Myc antibodies in whole cell extracts (Input). After IP with anti-Dor antibodies, only the co-immunoprecipitated full-length dVps16A protein (FL) or the C-terminal domain (-C) were detected by anti-Myc antibodies. (B,C) Myc-tagged truncated dVps16A proteins were co-expressed with Myc-Dor and in input samples detected with Myc antibodies. (B) After IP with anti-Dor antibodies, only dVps16A-C2 (-C2) and dVps16A-C3 (-C3) were co-immunoprecipitated as detected by anti-Myc antibodies, but not the shorter dVps16A-C1 (-C1). (C) After IP with anti-Dor antibodies, only the dVps16A-C (C) truncation co-immunoprecipitated, but not the shorter dVps16A-C2 or -C3 peptides. (D) Myc-tagged Dor and dVps16B were expressed alone or together in S2 cells. After IP with anti-Dor antibodies, dVps16B was only pulled down when co-expressed with Dor protein. (E) The summary of the co-immunoprecipitation results indicates that a small domain of dVps16A from amino acid 489 to 633 is required for binding to Dor.