Journal article
Interactome disassembly during apoptosis occurs independent of caspase cleavage
NE Scott, LD Rogers, A Prudova, NF Brown, N Fortelny, CM Overall, LJ Foster
Molecular Systems Biology | WILEY | Published : 2017
Abstract
Protein–protein interaction networks (interactomes) define the functionality of all biological systems. In apoptosis, proteolysis by caspases is thought to initiate disassembly of protein complexes and cell death. Here we used a quantitative proteomics approach, protein correlation profiling (PCP), to explore changes in cytoplasmic and mitochondrial interactomes in response to apoptosis initiation as a function of caspase activity. We measured the response to initiation of Fas-mediated apoptosis in 17,991 interactions among 2,779 proteins, comprising the largest dynamic interactome to date. The majority of interactions were unaffected early in apoptosis, but multiple complexes containing kno..
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Awarded by British Columbia Knowledge Development Fund
Funding Acknowledgements
CIHR Open Operating Grant (MOP-77688) to LJF provided financial support for this work. The Canada Foundation of Innovation, the British Columbia Knowledge Development Fund, and the BC Proteomics Network supported the mass spectrometry infrastructure used within the work. NES was supported by a Michael Smith Foundation Post-doctoral Fellowship (award # 5363) and a National Health and Medical Research Council of Australia (NHMRC) Overseas (Biomedical) Fellow (APP1037373). CMO is a Canada Research Chair in Proteinase Proteomics and Systems Biology. We would like to thank Dr. David Granville (UBC) for a kind gift of Compound 20.