The BioPlex Network: A Systematic Exploration of the Human Interactome


Protein interactions form a network whose structure drives cellular function and whose organization informs biological inquiry. Using high-throughput affinity-purification mass spectrometry, we identify interacting partners for 2,594 human proteins in HEK293T cells. The resulting network (BioPlex) contains 23,744 interactions among 7,668 proteins with 86% previously undocumented. BioPlex accurately depicts known complexes, attaining 80%-100% coverage for most CORUM complexes. The network readily subdivides into communities that correspond to complexes or clusters of functionally related proteins. More generally, network architecture reflects cellular localization, biological process, and molecular function, enabling functional characterization of thousands of proteins. Network structure also reveals associations among thousands of protein domains, suggesting a basis for examining structurally related proteins. Finally, BioPlex, in combination with other approaches, can be used to reveal interactions of biological or clinical significance. For example, mutations in the membrane protein VAPB implicated in familial amyotrophic lateral sclerosis perturb a defined community of interactors.

DOI: 10.1016/j.cell.2015.06.043

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@article{Huttlin2015TheBN, title={The BioPlex Network: A Systematic Exploration of the Human Interactome}, author={Edward L. Huttlin and Lily K.F. Ting and Raphael J. Bruckner and Fana Gebreab and Melanie P. Gygi and John Szpyt and Stanley Kui Fu Tam and Gabriela Zarraga and Greg Colby and Kurt Baltier and Rui Dong and Virginia Guarani and Laura Pontano Vaites and Alban Ordureau and Ramin Rezai Rad and Brian K. Erickson and Martin W{\"{u}hr and Joel M. Chick and Bo Zhai and Deepak Kolippakkam and Julian Mintseris and Robert A. Obar and Tim Harris and S. Artavanis-Tsakonas and Mathew E. Sowa and Pietro De Camilli and Joao A. Paulo and J Wade Harper and Steven P Gygi}, journal={Cell}, year={2015}, volume={162}, pages={425-440} }