From protein–protein complexes to interactomics

Abstract

Protein–protein interactions (or PPIs) are key elements for the normal functioning of a living cell. A large description of the protein interactomics field is given in this review where different aspects will be discussed. We first give an introduction of the different large scale experimental approaches from yeast two-hybrid to mass spectrometry used to discover PPIs and build protein interaction maps. Single PPI validation techniques such as co-immunoprecipitation or fluorescence methods are then presented as they are more and more integrated in global PPI discovery strategy. Data from different experimental sets are compared and an assessment of the different large scale technologies is presented. Bioinformatics tools can also predict with a good accuracy PPIs in silico, PPIs databases are now numerous and topological analysis has led to interesting insights into the nature of network connection. Finally, PPI, as an association of two proteins, has been structurally characterized for many protein complexes and is largely discussed throughout existing examples. The results obtained so far already provide the biologist with a large set of structured data from which knowledge on pathways and associated protein function can be extracted.