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MBC in Press, published online ahead of print August 1, 2007
Mol. Biol. Cell 10.1091/mbc.E07-04-0346

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Submitted on April 16, 2007
Revised on June 11, 2007
Accepted on July 19, 2007

Intrinsic Dynamic Behavior of Fascin in Filopodia

Yvonne S. Aratyn,* Thomas E. Schaus,* Edwin W. Taylor,* and Gary G. Borisy*{dagger}

*Department of Cell and Molecular Biology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611; {dagger}Marine Biological Laboratory, Woods Hole, MA 02543

Monitoring Editor: Josephine Adams

Recent studies showed that the actin cross-linking protein, fascin, undergoes rapid cycling between filopodial filaments. Here, we used an experimental and computational approach to dissect features of fascin exchange and incorporation in filopodia. Using expression of phospho-mimetic fascin mutants, we determined that fascin in the phosphorylated state is primarily freely diffusing, while actin bundling in filopodia is accomplished by fascin dephosphorylated at serine 39. Fluorescence recovery after photobleaching (FRAP) analysis revealed that fascin rapidly dissociates from filopodial filaments with a kinetic off-rate of 0.12 s-1, and undergoes diffusion at moderate rates with a coefficient of 6 µm2s-1. This kinetic off-rate was recapitulated in vitro, indicating that dynamic behavior is intrinsic to the fascin cross-linker. A computational reaction-diffusion model showed that reversible cross-linking is required for the delivery of fascin to growing filopodial tips at sufficient rates. Analysis of fascin bundling indicated that filopodia are semiordered bundles with one bound fascin per 25–60 actin monomers.

Address correspondence to: Yvonne S. Aratyn (y-aratyn{at}northwestern.edu)




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