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Fig. 7. The chimera HA-FYVE2-TOM1 behaves like a FYVE domain protein. (A) Schematic diagram of the chimeric construct HA-FYVE2-TOM1 where two FYVE domains derived from endofin were fused N-terminal to the full-length TOM1 coding sequence. HA-FYVE2-TOM1 causes aggregation/fusion of early endosomes but has no effect on the clathrin-associated adaptor proteins AP1, AP2 or AP3. A431 cells were transfected with HA-FYVE2-TOM1 and processed for immunofluorescence analysis by fixation with paraformaldehyde followed by permeabilization with either 0.1% Triton X-100 (B and C) or 0.05% saponin (D-F). The cells were stained with anti-HA (left panels and green in merged images) and anti-EEA1 (B), anti-endofin (C), anti-AP1 (D), anti-AP2 (E) or anti-AP3 (F) (middle panels and red in merged images on the right) and analyzed by confocal microscopy. Yellow in merged images represents areas of colocalization. CB, CB-I and CB-II, clathrin-binding sites; EBD, endofin-binding domain; GAT, GGAs and TOM1 homology; VHS, VPS-27, Hrs and STAM. Bar, 10 µm.





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