期刊
MOLECULAR SYSTEMS BIOLOGY
卷 11, 期 1, 页码 -出版社
WILEY
DOI: 10.15252/msb.20145504
关键词
forkhead box; mass spectrometry; protein-protein interaction; transcriptional factor
资金
- Computational Cancer Biology Training Program Fellowship, Cancer Prevention and Research Institute of Texas
- Jeffrey Lee Cousins Fellowship in Lung Cancer Research
- University of Texas MD Anderson Cancer Center
- U.S. Department of Defense [W81XWH-09-1-0409]
- National Institutes of Health [R01HG007538, CA016672]
- Center for Cancer Epigenetics and Sequencing and Microarray Facility [CA016672]
- MD Anderson Cancer Center
- NATIONAL CANCER INSTITUTE [P30CA016672] Funding Source: NIH RePORTER
- NATIONAL HUMAN GENOME RESEARCH INSTITUTE [R01HG007538] Funding Source: NIH RePORTER
- OFFICE OF THE DIRECTOR, NATIONAL INSTITUTES OF HEALTH [S10OD012304] Funding Source: NIH RePORTER
The current knowledge on how transcription factors (TFs), the ultimate targets and executors of cellular signalling pathways, are regulated by protein-protein interactions remains limited. Here, we performed proteomics analyses of soluble and chromatin-associated complexes of 56 TFs, including the targets of many signalling pathways involved in development and cancer, and 37 members of the Forkhead box (FOX) TF family. Using tandem affinity purification followed by mass spectrometry (TAP/MS), we performed 214 purifications and identified 2,156 high-confident protein-protein interactions. We found that most TFs form very distinct protein complexes on and off chromatin. Using this data set, we categorized the transcription-related or unrelated regulators for general or specific TFs. Our study offers a valuable resource of protein-protein interaction networks for a large number of TFs and underscores the general principle that TFs form distinct location-specific protein complexes that are associated with the different regulation and diverse functions of these TFs.
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