Molecular Biology of the Cell track citations

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
QUICK SEARCH:   [advanced]


     

Originally published as MBC in Press, 10.1091/mbc.E07-04-0346 on August 1, 2007

Vol. 18, Issue 10, 3928-3940, October 2007

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental Material
Right arrow All Versions of this Article:
E07-04-0346v1
18/10/3928    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Aratyn, Y. S.
Right arrow Articles by Borisy, G. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Aratyn, Y. S.
Right arrow Articles by Borisy, G. G.

Intrinsic Dynamic Behavior of Fascin in FilopodiaFormula

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; and {dagger}Marine Biological Laboratory, Woods Hole, MA 02543

Submitted April 16, 2007; Revised June 11, 2007; Accepted July 19, 2007
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 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.

This was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E07-04-0346) on August 1, 2007.

Formula The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).

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

Abbreviations used: FLIP, fluorescence loss in photobleaching; FRAP, fluorescence recovery after photobleaching; GFP, green fluorescent protein; RT, room temperature; TMR, tetramethylrhodamine; WT, wild type.




This article has been cited by other articles:


Home page
 Biophys. JHome page
M. Bathe, C. Heussinger, M. M. A. E. Claessens, A. R. Bausch, and E. Frey
Cytoskeletal Bundle Mechanics
Biophys. J., April 15, 2008; 94(8): 2955 - 2964.
[Abstract] [Full Text] [PDF]


Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Copyright © 2007 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.