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

Fengos, Georgios; Schmidt, Alexander; Martin, Katrin; Fluri, Erika; Aebersold, Ruedi; Iber, Dagmar; Pertz, Olivier (2014). Spatial proteomic and phospho-proteomic organization in three prototypical cell migration modes. Proteome Science, 12, p. 23. BioMed Central 10.1186/1477-5956-12-23

[img]
Preview
Text
art%3A10.1186%2F1477-5956-12-23.pdf - Published Version
Available under License Creative Commons: Attribution (CC-BY).

Download (5MB) | Preview

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.

Item Type:

Journal Article (Original Article)

Division/Institute:

08 Faculty of Science > Department of Biology > Institute of Cell Biology

UniBE Contributor:

Pertz, Olivier

Subjects:

500 Science > 570 Life sciences; biology

ISSN:

1477-5956

Publisher:

BioMed Central

Language:

English

Submitter:

Olivier Pertz

Date Deposited:

03 May 2016 10:20

Last Modified:

03 May 2016 10:20

Publisher DOI:

10.1186/1477-5956-12-23

PubMed ID:

24987309

Uncontrolled Keywords:

Directional cell migration; Fibroblast; Phosphorylation; Proteomics; Signaling

BORIS DOI:

10.7892/boris.81856

URI:

https://boris.unibe.ch/id/eprint/81856

Actions (login required)

Edit item Edit item
Provide Feedback