Membrane-mediated interaction drives mitochondrial ATPase assembly and cristae formation

Abstract

Cui reflects on new coarse-grained simulations demonstrating that mitochondrial ATP synthase dimers spontaneously self-associate.

Figure 1.

Membrane-mediated protein–protein interactions. Schematic illustration of protein organization in the mitochondrial cristae membranes (adapted from Fig. 5 of Davies et al., 2011); the ATP synthase dimers (yellow) assemble into rows along the cristae ridge, whereas proton pumps (green) residue predominantly in the at membrane regions. Such organization has been proposed to support a high local proton gradient (however, see the discussion by Rieger et al., 2014) and efficient ATP synthesis (Davies et al., 2011).

Figure 2.

Cone-shaped transmembrane proteins induce midplane membrane bending. Midplane membrane bending leads to long-range (5–500 nm) interactions (Phillips et al., 2009) between proteins. Note that although linear elasticity theory predicts repulsive interactions between proteins of similar isotropic shape (Kim et al., 1998; Weikl et al., 1998; Chou et al., 2001), attractive interactions may arise because of curvature anisotropy and deviation from linear elasticity (Chou et al., 2001; Reynwar et al., 2007).