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Elife. 2016 Jun 9;5. pii: e16950. doi: 10.7554/eLife.16950.

Global, quantitative and dynamic mapping of protein subcellular localization.

Author information

1
Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany.

Abstract

Subcellular localization critically influences protein function, and cells control protein localization to regulate biological processes. We have developed and applied Dynamic Organellar Maps, a proteomic method that allows global mapping of protein translocation events. We initially used maps statically to generate a database with localization and absolute copy number information for over 8700 proteins from HeLa cells, approaching comprehensive coverage. All major organelles were resolved, with exceptional prediction accuracy (estimated at >92%). Combining spatial and abundance information yielded an unprecedented quantitative view of HeLa cell anatomy and organellar composition, at the protein level. We subsequently demonstrated the dynamic capabilities of the approach by capturing translocation events following EGF stimulation, which we integrated into a quantitative model. Dynamic Organellar Maps enable the proteome-wide analysis of physiological protein movements, without requiring any reagents specific to the investigated process, and will thus be widely applicable in cell biology.

KEYWORDS:

EGF signalling; cell biology; computational biology; human; map of the cell; organellar proteomics; protein translocations; spatial proteomics; subcellular localization; systems biology

PMID:
27278775
PMCID:
PMC4959882
DOI:
10.7554/eLife.16950
[Indexed for MEDLINE]
Free PMC Article

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