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Published on: May 19, 2016
Serine phosphorylation regulates paxillin turnover during cell migration
Nancy Abou Zeid1, Ana-Maria Vallés, Brigitte Boyer
1Institut Curie, CNRS UMR146, Centre Universitaire, Orsay, France. nancy.abouzeid@curie.u-psud.fr
Cell Communication and Signaling : CCS
|November 24, 2006
Summary
Paxillin phosphorylation at serines 188/190 protects it from degradation during cell migration. This serine-regulated degradation controls cell motility and membrane dynamics.
Area of Science:
- Cell Biology
- Molecular Biology
Background:
- Paxillin is a focal adhesion adaptor protein regulated by phosphorylation during cell migration.
- Phosphorylation of paxillin at serines 188 and 190 is induced by extracellular matrix adhesion but its function is unknown.
Purpose of the Study:
- To determine the role of paxillin phosphorylation at serine residues 188 and 190 in regulating cell migration.
Main Methods:
- Utilized NBT-II epithelial cells and an EGFP-tagged paxillin mutant (S188/190A) to investigate phosphorylation.
- Examined paxillin's interaction with proteasomal degradation pathways.
- Assessed cell spreading, protrusive activity, and migration rates.
Main Results:
- Paxillin is regulated by proteasomal degradation following polyubiquitylation.
- Collagen-induced cell migration protects paxillin from degradation.
- Phosphorylation of paxillin serines 188/190 is essential for this protective effect.
- Cells with non-phosphorylatable paxillin (S188/190A) exhibit reduced spreading and protrusion but enhanced migration.
Conclusions:
- Paxillin degradation, regulated by serine phosphorylation, is a key mechanism controlling cell motility.
- This pathway modulates membrane dynamics, impacting overall cell migration efficiency.
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