TY - JOUR T1 - Specificity and Evolvability in Eukaryotic Protein Interaction Networks A1 - Beltrao, Pedro A1 - Serrano, Luis Y1 - 2007/02/16 N2 -
To understand how the cell performs the required biological functions and reacts to changes in the environment, scientists have been studying how cellular components interact. In recent years, new experimental methods have immensely increased our ability to map out these connections. However, it is important to keep in mind that biological systems are constantly evolving to cope with environmental changes. What then is the impact of the genomic variability brought by point mutations, segmental duplications, etc., on these interaction networks? We have tried here to quantify the rate by which protein interactions changed during the evolution of eukaryotic cells. According to the authors, about 0.5% to 3% of the interactions can change every million years. Also, protein properties, such as binding specificity (defined as the number of binding surfaces or binding partners) and protein function, help determine the rate of interaction turnover. This work suggests that protein interactions are evolutionarily plastic and the fact that a group of proteins has been conserved in different genomes does not mean that their interaction repertoire and functions are necessarily conserved. This work emphasizes the importance of studying biological systems in the context of evolutionary change.