TableEdit

Ewing, RM, Chu, P, Elisma, F, Li, H, Taylor, P, Climie, S, McBroom-Cerajewski, L, Robinson, MD, O'Connor, L, Li, M, Taylor, R, Dharsee, M, Ho, Y, Heilbut, A, Moore, L, Zhang, S, Ornatsky, O, Bukhman, YV, Ethier, M, Sheng, Y, Vasilescu, J, Abu-Farha, M, Lambert, JP, Duewel, HS, Stewart, II, Kuehl, B, Hogue, K, Colwill, K, Gladwish, K, Muskat, B, Kinach, R, Adams, SL, Moran, MF, Morin, GB, Topaloglou, T and Figeys, D (2007) Large-scale mapping of human protein-protein interactions by mass spectrometry. Mol. Syst. Biol. 3:89

Mapping protein-protein interactions is an invaluable tool for understanding protein function. Here, we report the first large-scale study of protein-protein interactions in human cells using a mass spectrometry-based approach. The study maps protein interactions for 338 bait proteins that were selected based on known or suspected disease and functional associations. Large-scale immunoprecipitation of Flag-tagged versions of these proteins followed by LC-ESI-MS/MS analysis resulted in the identification of 24,540 potential protein interactions. False positives and redundant hits were filtered out using empirical criteria and a calculated interaction confidence score, producing a data set of 6463 interactions between 2235 distinct proteins. This data set was further cross-validated using previously published and predicted human protein interactions. In-depth mining of the data set shows that it represents a valuable source of novel protein-protein interactions with relevance to human diseases. In addition, via our preliminary analysis, we report many novel protein interactions and pathway associations.

PubMed PMC1847948 Online version:10.1038/msb4100134

Humans; Immunoprecipitation; Protein Binding; Proteins/metabolism; Spectrometry, Mass, Electrospray Ionization/methods