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Fig. 3. A small domain in dVps16A is required for binding to Car. The binding of different dVps16A truncations (outlined in panel E) to Car was evaluated by co-immunoprecipitation experiments. (A) HA-tagged truncations of dVps16A were co-expressed with HA-Car and in whole cell extracts (input) detected with HA antibodies. After IP with anti-Car antibodies only dVps16A-C was co-immunoprecipitated. (B) HA- or Myc-tagged truncations of dVps16A were co-expressed with HA-Car protein and detected in input samples with anti-Vps16 antibodies. After IP with anti-dVps16A antibodies, HA-Car was co-immunoprecipitated only with full-length dVps16A or dVps16A-C. (C) HA-tagged Rop, dVps33B or Car were co-expressed in S2 cells with the Myc-tagged dVsp16A-C domain and detected in input samples with anti-dVps16A or anti-HA antibodies. After IP with anti-dVsp16A antibodies, proteins were detected with anti-HA antibodies. (D) Myc-tagged truncations of dVps16 were co-expressed with HA-Car. After IP with anti-Myc antibodies co-precipitated Car was detected with anti-Car antibodies. (E) The summary of the co-immunoprecipitation results indicates that only a small domain of dVps16A from aa 489-555 is required for binding to Car.





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