期刊
CELL SYSTEMS
卷 5, 期 4, 页码 399-+出版社
CELL PRESS
DOI: 10.1016/j.cels.2017.09.011
关键词
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资金
- Science Foundation Ireland
- Health Research Board
- Wellcome Trust under the SFI-HRB-Wellcome Trust Biomedical Research Partnership [103049/Z/13/Z]
- Science Foundation Ireland [06/CE/B1129, 15/CDA/3495]
- European Union FP7 Grant [278568]
- Cancer Research UK [C347/A8363]
- Breast Cancer Now
- NHS
- Wellcome Trust [103049/Z/13/Z] Funding Source: Wellcome Trust
- Science Foundation Ireland (SFI) [15/CDA/3495] Funding Source: Science Foundation Ireland (SFI)
- Cancer Research UK [14276, 24439, 25237] Funding Source: researchfish
Protein complexes are responsible for the bulk of activities within the cell, but how their behavior and abundance varies across tumors remains poorly understood. By combining proteomic profiles of breast tumors with a large-scale protein-protein interaction network, we have identified a set of 285 high-confidence protein complexes whose subunits have highly correlated protein abundance across tumor samples. We used this set to identify complexes that are reproducibly under-or overexpressed in specific breast cancer subtypes. We found that mutation or deletion of one subunit of a co-regulated complex was often associated with a collateral reduction in protein expression of additional complex members. This collateral loss phenomenon was typically evident from proteomic, but not transcriptomic, profiles, suggesting post-transcriptional control. Mutation of the tumor suppressor E-cadherin (CDH1) was associated with a collateral loss of members of the adherens junction complex, an effect we validated using an engineered model of E-cadherin loss.
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