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Figure 5


Fig. 5. The ABBA IM domain interacts with PtdIns(4,5)P2-rich membranes and deforms them into tubular structures. (A) ABBA IM domain (ABBA-IMD) or ABBA-IMDmut were incubated in the absence or presence of vesicles. After centrifugation, equal amounts of supernatant `S' and pellet `P' were analysed on SDS-PAGE. ABBA-IMD bound PtdIns(4,5)P2-containing vesicles with high affinity, whereas ABBA-mutIMD displayed a severe defect in PtdIns(4,5)P2 binding. (B) Quantification of wild-type ABBA-IMD and ABBA-mutIMD binding to lipid vesicles from three individual experiments. Data are represented as mean ± s.e.m. (C) Electron micrographs of vesicles containing 30% PtdIns(4,5)P2 mixed with buffer, ABBA-IMD or ABBA-IMDmut. Only wild-type ABBA-IMD induced clustering of vesicles and membrane tubulation. (D) Micrographs of different magnifications showing that ABBA-IMD induced membrane tubules of vesicles containing 5% PtdIns(4,5)P2. Scale bars: 1 µm in C, upper row; 0.2 µm in C, bottom row; 0.5 µm (left) and 0.2 µm (middle and right) in D.





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