Journal
JOURNAL OF PROTEOME RESEARCH
Volume 11, Issue 12, Pages 6080-6101Publisher
AMER CHEMICAL SOC
DOI: 10.1021/pr300736v
Keywords
quantitative proteomics; mass spectrometry; breast cancer; MCF7 cells; subcellular organelles; subcellular location; nucleus; mitochondria; TCA cycle; oxidative phosphorylation; glycolysis
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Funding
- Wellcome Trust
- King Faisal Foundation
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Concurrent proteomics analysis of the nuclei and mitochondria of MCF7 breast cancer cells identified 985 proteins (40% of all detected proteins) present in both organelles. Numerous proteins from all five complexes involved in oxidative phosphorylation(e.g., NDUFA5, NDUFB10, NDUFS1, NDUF2, SDHA, UQRB, UQRC2, UQCRH, COMA, COX5B, MT-CO2, ATP5A1, ATP5B, ATP5H; etc.), from the TCA-cycle SUCLAG2, etc.), and from glycolysis (ALDOA, ENO1, FBP1, GPI, PGK1, TALDO1, etc.) were distributed to both the nucleus and mitochondria. In contrast, Proteins involved in nuclear/mitochondrial RNA processing/translation and Ras/Rab signaling showed different partitioning patterns. The identity of the OxPhos, TCA-cycle, and glycolysis proteins distributed to both the nucleus and mitochondria provides evidence for spatio-functional integration of these processes over the two different subcellular organelles.We suggest that there are unrecognized aspects of functional coordination between the nucleus'. and mitochondria;I: that integration of Core functional processes via wide subcellular distribution of constituent proteins is a common characteristic of cells, and that subcellular spatial integration of function may be a vital aspect of cancer.
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