Abstract：
:Elucidation of endogenous cellular protein-protein interactions and their networks is most desirable for biological studies. Here we report our study of endogenous human coregulator protein complex networks obtained from integrative mass spectrometry-based analysis of 3290 affinity purifications. By preserving weak protein interactions during complex isolation and utilizing high levels of reciprocity in the large dataset, we identified many unreported protein associations, such as a transcriptional network formed by ZMYND8, ZNF687, and ZNF592. Furthermore, our work revealed a tiered interplay within networks that share common proteins, providing a conceptual organization of a cellular proteome composed of minimal endogenous modules (MEMOs), complex isoforms (uniCOREs), and regulatory complex-complex interaction networks (CCIs). This resource will effectively fill a void in linking correlative genomic studies with an understanding of transcriptional regulatory protein functions within the proteome for formulation and testing of future hypotheses.
journal_name
Celljournal_title
Cellauthors
Malovannaya A,Lanz RB,Jung SY,Bulynko Y,Le NT,Chan DW,Ding C,Shi Y,Yucer N,Krenciute G,Kim BJ,Li C,Chen R,Li W,Wang Y,O'Malley BW,Qin Jdoi
10.1016/j.cell.2011.05.006subject
Has Abstractpub_date
2011-05-27 00:00:00pages
787-99issue
5eissn
0092-8674issn
1097-4172pii
S0092-8674(11)00532-0journal_volume
145pub_type
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