Related Experiment Videos
Modulation of cell spreading and migration by pp125FAK phosphorylation
S Sankar1, N Mahooti-Brooks, G Hu
1Department of Pathology, Yale University School of Medicine, New Haven, Connecticut 06510, USA.
The American Journal of Pathology
|September 1, 1995
Summary
Cell migration speed is regulated by tyrosine phosphorylation of focal adhesion kinase (FAK). Higher FAK phosphorylation reduces migration, while lower levels increase it, impacting cell movement on different matrices.
Area of Science:
- Cell Biology
- Biochemistry
- Molecular Biology
Background:
- Cell migration is crucial for various biological processes.
- Integrin-mediated signaling and focal adhesion kinase (FAK) are implicated in cell migration.
- Extracellular matrix (ECM) composition influences cell behavior.
Purpose of the Study:
- To investigate the role of pp125FAK tyrosine phosphorylation in modulating cell migration.
- To determine the influence of extracellular matrix (ECM) and pp60v-src on FAK phosphorylation and cell migration.
Main Methods:
- Cells were plated on different ECM substrates (type I collagen, fibronectin).
- Tyrosine phosphorylation levels of pp125FAK were analyzed.
- Cell spreading and migration rates were measured.
- The effect of pp60v-src expression on cell migration and FAK phosphorylation was assessed.
Main Results:
- Enhanced pp125FAK tyrosine phosphorylation correlated with increased cell spreading and decreased migration.
- Cells on type I collagen showed less spreading, lower FAK phosphorylation, and faster migration compared to cells on fibronectin.
- pp60v-src expression modulated pp125FAK phosphorylation and altered cell migration rates.
Conclusions:
- pp125FAK tyrosine phosphorylation is a key regulator of cell migration.
- ECM composition and tyrosine kinase activity (pp60v-src) influence cell migration through FAK phosphorylation.
- FAK phosphorylation is integral to the signaling pathways governing ECM-modulated, integrin-mediated cell migration.