Different cellular states change the expression and localization of proteins targeting mitochondria [22] . To analyze the systemic properties of the mt proteome under the dysfunctional r 0 state, we constructed a network of reliable mt proteins. By using information about the physical and functional links of these proteins, we could map 726 out of 770 reliable mt proteins into a major network (right panel in Figure 1A ; see Materials and Methods for details). The remaining 44 proteins disconnected from the major network were excluded from further network analysis. We discovered that the network is divided into two prominent subnetworks of upregulated (green) and down-regulated proteins (red) based on abundance ratios (Figure 2A ). Interestingly, more links were made