Spatial proteomic and phospho-proteomic organization in three prototypical cell migration modes

Proteome Science

Olivier Pertz¹  Dagmar Iber²  Ruedi Aebersold⁴  Erika Fluri¹  Katrin Martin¹  Alexander Schmidt³  Georgios Fengos² 

[1]Department Biomedicine, University of Basel, Mattenstrasse 28, CH-4058 Basel, Switzerland

[2]ETH Zurich, D-BSSE, Mattenstrasse 26, CH-4058 Basel, Switzerland

[3]University of Basel, Biozentrum, Klingelbergstrasse 50/70, CH-4056 Basel, Switzerland

[4]University of Zurich, Faculty of Science, Zurich, Switzerland

关键词: Phosphorylation;    Proteomics;    Signaling;    Directional cell migration;    Fibroblast;   

Others  :  816497
DOI  :  10.1186/1477-5956-12-23

 received in 2013-12-19, accepted in 2014-04-25,  发布年份 2014

【 摘 要 】

Background

Tight spatio-temporal signaling of cytoskeletal and adhesion dynamics is required for localized membrane protrusion that drives directed cell migration. Different ensembles of proteins are therefore likely to get recruited and phosphorylated in membrane protrusions in response to specific cues.

Results

Here, we use an assay that allows to biochemically purify extending protrusions of cells migrating in response to three prototypical receptors: integrins, recepor tyrosine kinases and G-coupled protein receptors. Using quantitative proteomics and phospho-proteomics approaches, we provide evidence for the existence of cue-specific, spatially distinct protein networks in the different cell migration modes.

Conclusions

The integrated analysis of the large-scale experimental data with protein information from databases allows us to understand some emergent properties of spatial regulation of signaling during cell migration. This provides the cell migration community with a large-scale view of the distribution of proteins and phospho-proteins regulating directed cell migration.

【 授权许可】

   
2014 Fengos et al.; licensee BioMed Central Ltd.

【 图 表 】

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