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Antagonism between Ena/VASP proteins and actin filament capping regulates fibroblast motility

James E Bear1, Tatyana M Svitkina, Matthias Krause

  • 1Massachusetts Institute of Technology, Department of Biology, Cambridge 02139, USA.

Cell
|June 28, 2002
PubMed

Insights

Ena/VASP proteins influence cell motility by regulating actin filament structure. Their absence leads to slower but more persistent lamellipodial protrusion, impacting overall cell movement.

Area of Science:

  • Cell Biology
  • Biochemistry

Background:

  • Cell motility is crucial for biological processes and relies on lamellipodial protrusion driven by actin polymerization.
  • Ena/VASP proteins are known to promote actin-driven motility in pathogens like Listeria but paradoxically inhibit cell translocation.

Purpose of the Study:

  • To investigate the dual role of Ena/VASP proteins in lamellipodial protrusion and cell motility.
  • To elucidate how Ena/VASP proteins affect the actin cytoskeleton during cell movement.

Main Methods:

  • Analysis of Ena/VASP-deficient and Ena/VASP-overexpressing cells.
  • Microscopic examination of lamellipodial dynamics and actin network architecture.
  • In vitro biochemical assays to determine Ena/VASP interaction with actin filaments.

Main Results:

  • Ena/VASP-deficient lamellipodia exhibited slower, more persistent protrusion and altered actin networks with shorter, branched filaments.
  • Excess Ena/VASP resulted in longer, less branched actin filaments within lamellipodia.
  • In vitro studies confirmed Ena/VASP promotes actin filament elongation by interacting with barbed ends.

Conclusions:

  • Ena/VASP proteins play a critical role in regulating cell motility by modulating the geometry of actin filament networks within lamellipodia.
  • The findings resolve the paradox of Ena/VASP's opposing effects on pathogen and host cell motility.

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