| Literature DB >> 33961781 |
Edward L Huttlin1, Raphael J Bruckner2, Jose Navarrete-Perea2, Joe R Cannon2, Kurt Baltier2, Fana Gebreab2, Melanie P Gygi2, Alexandra Thornock2, Gabriela Zarraga2, Stanley Tam2, John Szpyt2, Brandon M Gassaway2, Alexandra Panov2, Hannah Parzen2, Sipei Fu2, Arvene Golbazi2, Eila Maenpaa2, Keegan Stricker2, Sanjukta Guha Thakurta2, Tian Zhang2, Ramin Rad2, Joshua Pan3, David P Nusinow2, Joao A Paulo2, Devin K Schweppe2, Laura Pontano Vaites2, J Wade Harper4, Steven P Gygi5.
Abstract
Thousands of interactions assemble proteins into modules that impart spatial and functional organization to the cellular proteome. Through affinity-purification mass spectrometry, we have created two proteome-scale, cell-line-specific interaction networks. The first, BioPlex 3.0, results from affinity purification of 10,128 human proteins-half the proteome-in 293T cells and includes 118,162 interactions among 14,586 proteins. The second results from 5,522 immunoprecipitations in HCT116 cells. These networks model the interactome whose structure encodes protein function, localization, and complex membership. Comparison across cell lines validates thousands of interactions and reveals extensive customization. Whereas shared interactions reside in core complexes and involve essential proteins, cell-specific interactions link these complexes, "rewiring" subnetworks within each cell's interactome. Interactions covary among proteins of shared function as the proteome remodels to produce each cell's phenotype. Viewable interactively online through BioPlexExplorer, these networks define principles of proteome organization and enable unknown protein characterization.Entities:
Keywords: AP-MS; BioPlex; bioinformatics; cell specificity; computational biology; human interactome; network biology; protein interactions; proteomics; proteotypes
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Year: 2021 PMID： 33961781 PMCID： PMC8165030 DOI： 10.1016/j.cell.2021.04.011
Source DB: PubMed Journal: Cell ISSN： 0092-8674 Impact factor: 66.850