Fig. 4.
Oligomerization via a new interface between the KPF loop and the helical domain. (A) Two views on the EHD4ΔN oligomers in the crystals represented by two dimers. One dimer is colored as in Fig. 1E, whereas the other is colored in light blue. Note the gap between the G interfaces of assembling dimers (Right). (B) Inset shows details of the oligomerization surface involving the KPF loop and the helical domain of the opposing dimer. (C) Liposome tubulation of EHD4ΔN, EHD4ΔN F125A and EHD4ΔN K302A/R305A, as in Fig. 1B. (D) Basic and stimulated ATP hydrolysis reactions of EHD4ΔN F125A and EHD4ΔN K302A/R305A were carried out as in Fig. 1C. (E) Expression of mCherry-tagged EHD4ΔN F125A and EHD4ΔN K302A/R305A in HeLa cells, as in Fig. 1D. (Scale bars: C, 500 nm; E, 10 μm.)