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.
%0 Journal Article
%1 Huttlin2016BioPlex
%A Huttlin, Edward L.
%A Ting, Lily
%A Bruckner, Raphael J.
%A Gebreab, Fana
%A Gygi, Melanie P.
%A Szpyt, John
%A Tam, Stanley
%A Zarraga, Gabriela
%A Colby, Greg
%A Baltier, Kurt
%A Dong, Rui
%A Guarani, Virginia
%A Vaites, Laura P.
%A Ordureau, Alban
%A Rad, Ramin
%A Erickson, Brian K.
%A Wühr, Martin
%A Chick, Joel
%A Zhai, Bo
%A Kolippakkam, Deepak
%A Mintseris, Julian
%A Obar, Robert A.
%A Harris, Tim
%A Artavanis-Tsakonas, Spyros
%A Sowa, Mathew E.
%A De Camilli, Pietro
%A Paulo, Joao A.
%A Harper, J. Wade
%A Gygi, Steven P.
%D 2016
%I Elsevier
%J Cell
%K protein-function protein-protein-interactions
%N 2
%P 425--440
%R 10.1016/j.cell.2015.06.043
%T The BioPlex Network: A Systematic Exploration of the Human Interactome
%U http://dx.doi.org/10.1016/j.cell.2015.06.043
%V 162
%X 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.
@article{Huttlin2016BioPlex,
abstract = {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.},
added-at = {2018-12-02T16:09:07.000+0100},
author = {Huttlin, Edward L. and Ting, Lily and Bruckner, Raphael J. and Gebreab, Fana and Gygi, Melanie P. and Szpyt, John and Tam, Stanley and Zarraga, Gabriela and Colby, Greg and Baltier, Kurt and Dong, Rui and Guarani, Virginia and Vaites, Laura P. and Ordureau, Alban and Rad, Ramin and Erickson, Brian K. and W\"{u}hr, Martin and Chick, Joel and Zhai, Bo and Kolippakkam, Deepak and Mintseris, Julian and Obar, Robert A. and Harris, Tim and Artavanis-Tsakonas, Spyros and Sowa, Mathew E. and De Camilli, Pietro and Paulo, Joao A. and Harper, J. Wade and Gygi, Steven P.},
biburl = {https://www.bibsonomy.org/bibtex/2405a9301c5b87476b172010e4e31ba5e/karthikraman},
citeulike-article-id = {13674768},
citeulike-linkout-0 = {http://www.cell.com/cell/abstract/S0092-8674(15)00768-0},
citeulike-linkout-1 = {http://dx.doi.org/10.1016/j.cell.2015.06.043},
day = 15,
doi = {10.1016/j.cell.2015.06.043},
interhash = {e6c821650082f79618cc14f1196270b0},
intrahash = {405a9301c5b87476b172010e4e31ba5e},
issn = {00928674},
journal = {Cell},
keywords = {protein-function protein-protein-interactions},
month = mar,
number = 2,
pages = {425--440},
posted-at = {2015-11-10 10:12:24},
priority = {2},
publisher = {Elsevier},
timestamp = {2018-12-02T16:09:07.000+0100},
title = {The {BioPlex} Network: A Systematic Exploration of the Human Interactome},
url = {http://dx.doi.org/10.1016/j.cell.2015.06.043},
volume = 162,
year = 2016
}