TY - JOUR
T1 - The BioPlex Network
T2 - A Systematic Exploration of the Human Interactome
AU - Huttlin, Edward L.
AU - Ting, Lily
AU - Bruckner, Raphael J.
AU - Gebreab, Fana
AU - Gygi, Melanie P.
AU - Szpyt, John
AU - Tam, Stanley
AU - Zarraga, Gabriela
AU - Colby, Greg
AU - Baltier, Kurt
AU - Dong, Rui
AU - Guarani, Virginia
AU - Vaites, Laura Pontano
AU - Ordureau, Alban
AU - Rad, Ramin
AU - Erickson, Brian K.
AU - Wühr, Martin
AU - Chick, Joel
AU - Zhai, Bo
AU - Kolippakkam, Deepak
AU - Mintseris, Julian
AU - Obar, Robert A.
AU - Harris, Tim
AU - Artavanis-Tsakonas, Spyros
AU - Sowa, Mathew E.
AU - De Camilli, Pietro
AU - Paulo, Joao A.
AU - Harper, J. Wade
AU - Gygi, Steven P.
N1 - Publisher Copyright:
© 2015 Elsevier Inc.
PY - 2015/7/18
Y1 - 2015/7/18
N2 - Summary 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.
AB - Summary 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.
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U2 - 10.1016/j.cell.2015.06.043
DO - 10.1016/j.cell.2015.06.043
M3 - Article
C2 - 26186194
AN - SCOPUS:84937213168
SN - 0092-8674
VL - 162
SP - 425
EP - 440
JO - Cell
JF - Cell
IS - 2
M1 - 8290
ER -