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VASP dynamics during lamellipodia protrusion

Nature Cell Biology volume 1, pages 321–322 (1999)Cite this article

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The continuous remodelling of the actin cytoskeleton is a prerequisite for many cells to move and alter their shape. These activities are dependent on the highly regulated and site-specific formation of protein complexes that act as adaptors to link external signals with actin assembly. The members of the Ena/VASP protein family, VASP (for vasodilator-stimulated phosphoprotein), Mena and Evl, have been implicated in the temporal and spatial control of actin-filament dynamics. These proteins not only localize to sites of actin assembly, such as focal-adhesion sites, membrane ruffles and neuronal growth cones1,2,3, but are also involved in platelet aggregation4, axon guidance5 and the actin-based motility of the intracellular bacterial pathogen Listeria monocytogenes2,6,7,8. By generating a stable melanoma cell line expressing VASP fused to green fluorescent protein (GFP), we now show that VASP not only co-localizes to adhesion sites with the adaptor proteins vinculin and zyxin (ref. 3 and data not shown), but is also recruited to the tips of lamellipodia in amounts that are directly proportional to the rate of protrusion. These data indicate that VASP may be an adaptor molecule involved in actin-based cell motility. They also raise important questions about the spatial relationships of the different components earmarked to have roles in actin-filament dynamics.

In contrast, the scan of GFP–VASP intensity showed a sharp peak at the lamellipodium front and a smaller peak at the rear. The latter peak arose from the presence of VASP in the focal complexes that accompany the base of rapidly migrating lamellipodia. The appearance of VASP in a line at the cell front was seen only in protruding, and not in retracting, lamellipodia (see Supplementary Information ). Measurements (taken from the video frames) of the GFP fluorescence intensity at the tips of lamellipodia as a function of transient protrusion rate indicated that there was a linear relationship between these two variables (Fig. 1c).

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Figure 1: Comparison of VASP and F-actin distribution in protruding lamellipodia.
Figure 2: GFP–VASP is localized at the tips of lamellipodia and microspikes/filopodia.

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Acknowledgements

We thank M. Schmittner for technical assistance and photography, E. Eppacher for manuscript processing and T. Stradal for help with statistics. This work was funded in part by the Austrian Science Research Foundation, the Austrian National Bank and the Seegen Stiftung of the Austrian Academy of Sciences (to J.V.S) and in part by the Deutsche Forschungsgemeinschaft and the Fonds der Chemische Industrie (to J.W.).

Correspondence and requests for materials should be addressed to J.V.S.

Supplementary Information is available on Nature Cell Biology’s World-Wide Web site (http://cellbio.nature.com).

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Authors and Affiliations

  1. Institute of Molecular Biology, Austrian Academy of Sciences, Billrothstrasse 11, Salzburg, A-5020, Austria

    Klemens Rottner & J.Victor Small

  2. Abteilung Zellbiologie, Gesellschaft für Biotechnologische Forschung, Mascheroder Weg 1, Braunschweig, D-38124, Germany

    Barbara Behrendt & Jurgen Wehland

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  1. Klemens Rottner
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Rottner, K., Behrendt, B., Small, J. et al. VASP dynamics during lamellipodia protrusion . Nat Cell Biol 1, 321–322 (1999). https://doi.org/10.1038/13040

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