Spatial proteomic and phospho-proteomic organization in three prototypical cell migration modes
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BORIS DOI
Date of Publication
2014
Publication Type
Article
Division/Institute
Author
Fengos, Georgios | |
Schmidt, Alexander | |
Martin, Katrin | |
Fluri, Erika | |
Aebersold, Ruedi | |
Iber, Dagmar |
Subject(s)
Series
Proteome Science
ISSN or ISBN (if monograph)
1477-5956
Publisher
BioMed Central
Language
English
Publisher DOI
PubMed ID
24987309
Uncontrolled Keywords
Description
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.
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.
File(s)
File | File Type | Format | Size | License | Publisher/Copright statement | Content | |
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art%3A10.1186%2F1477-5956-12-23.pdf | text | Adobe PDF | 5.46 MB | published |