Figure 1: Membrane binding by the complexin CTD is curvature dependent.
From: Membrane curvature sensing by the C-terminal domain of complexin
(a) Sequence of worm complexin highlighting three discrete motifs in the CTD: the C-terminal motif (CT motif, green), the amphipathic motif (AH motif, orange) and the second amphipathic motif (AH2, blue). (b) NMR intensity ratios (the ratio of resonance intensity in the presence of vesicles to that in their absence) for 100 μM full-length WT worm complexin in the presence of 13.5 mM LUV lipids (red) and 1 mM SUV lipids (black) in 100 mM NaCl. (c) The average bound fraction of residues in the AH motif (residues 110–124) and CT motif (residues 128–143) of 100 μM full-length WT worm complexin for 85/15 POPC/POPS LUVs compared with SUVs at different concentrations and of different compositions. Black asterisks denote a significant difference (P<0.01, n=15). Differences between LUV and 1 mM SUV for CT motif, between 3 mM 85/15 SUV and 3 mM 70/30 SUV for the AH motif, and between any of the 3 mM SUV CT motif data are not significant (n=15). (d) Bound fraction of the AH and CT motifs of 75 μM full-length WT worm complexin for 70/30 POPC/POPS LUVs in negligible salt compared with LUVs of different compositions and at higher salt concentrations. Black/blue asterisks denote a significant difference (P<0.01) from the 10 mM 70/30 LUV AH (black, n=14) or CT (blue, n=15) motif.
