Proteome-Wide Analysis of Protein Abundance and Turnover
Wellcome Open Research 2018, 3:51 Last updated: 09 MAY 2018 RESEARCH ARTICLE Proteome-wide analysis of protein abundance and turnover remodelling during oncogenic transformation of human breast epithelial cells [version 1; referees: awaiting peer review] Tony Ly 1-3*, Aki Endo1,2,4*, Alejandro Brenes1,2, Marek Gierlinski1,2, Vackar Afzal1,2, Andrea Pawellek1,2, Angus I. Lamond1,2 1Centre for Gene Regulation and Expression, University of Dundee, Dundee, UK 2Laboratory for Quantitative Proteomics, University of Dundee, Dundee, UK 3Wellcome Centre for Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh, UK 4Cell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, Tokyo, Japan * Equal contributors v1 First published: 02 May 2018, 3:51 (doi: 10.12688/wellcomeopenres.14392.1) Open Peer Review Latest published: 02 May 2018, 3:51 (doi: 10.12688/wellcomeopenres.14392.1) Referee Status: AWAITING PEER Abstract Background: Viral oncogenes and mutated proto-oncogenes are potent REVIEW drivers of cancer malignancy. Downstream of the oncogenic trigger are alterations in protein properties that give rise to cellular transformation and the Discuss this article acquisition of malignant cellular phenotypes. Developments in mass Comments (0) spectrometry enable large-scale, multidimensional characterisation of proteomes. Such techniques could provide an unprecedented, unbiased view of how oncogene activation remodels a human cell proteome. Methods: Using quantitative MS-based proteomics and cellular assays, we analysed how transformation induced by activating v-Src kinase remodels the proteome and cellular phenotypes of breast epithelial (MCF10A) cells. SILAC MS was used to comprehensively characterise the MCF10A proteome and to measure v-Src-induced changes in protein abundance across seven time-points (1-72 hrs).
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