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dc.contributor.authorAratyn, Yvonne S.  Concept link
dc.contributor.authorSchaus, Thomas E.  Concept link
dc.contributor.authorTaylor, Edwin W.  Concept link
dc.contributor.authorBorisy, Gary G.  Concept link
dc.date.accessioned2007-10-30T15:10:35Z
dc.date.available2007-10-30T15:10:35Z
dc.date.issued2007-08-01
dc.identifier.citationMolecular Biology of the Cell 18 (2007): 3928-3940en
dc.identifier.urihttps://hdl.handle.net/1912/1839
dc.descriptionAuthor Posting. © American Society for Cell Biology, 2007. This article is posted here by permission of American Society for Cell Biology for personal use, not for redistribution. The definitive version was published in Molecular Biology of the Cell 18 (2007): 3928-3940, doi:10.1091/mbc.E07-04-0346.en
dc.description.abstractRecent 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 phosphomimetic fascin mutants, we determined that fascin in the phosphorylated state is primarily freely diffusing, whereas actin bundling in filopodia is accomplished by fascin dephosphorylated at serine 39. Fluorescence recovery after photobleaching analysis revealed that fascin rapidly dissociates from filopodial filaments with a kinetic off-rate of 0.12 s–1 and that it 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.en
dc.description.sponsorshipThis work was supported by a National Institutes of Health F31National Research Service Award NS055565-01 (to Y.S.A.), Northwestern University Pulmonary and Critical Care Division T32 (to T.E.S.), and National Institutes of Health grant GM-70898 (to G.G.B.).en
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dc.language.isoen_USen
dc.publisherAmerican Society for Cell Biologyen
dc.relation.urihttps://doi.org/10.1091/mbc.E07-04-0346
dc.titleIntrinsic dynamic behavior of fascin in filopodiaen
dc.typeArticleen
dc.identifier.doi10.1091/mbc.E07-04-0346


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