Publications
Vincent Noireaux
ActA and the Human Zyxin Harbour Arp2/3 Complex Independent Actin Polymerisation ActivityJ. Fradelizi, V. Noireaux, J. Plastino, B. Menichi, D. Louvard, C. Sykes, R.M. Golsteyn, E. Friederich, Nature Cell Biology 3, 699-707
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Abstract
The actin cytoskeleton is a dynamic network that is composed of a variety of F-actin structures. To understand how these structures are produced, we tested the capacity of proteins to direct actin polymerization in a bead assay in vitro and in a mitochondrial-targeting assay in cells. We found that human zyxin and the related protein ActA of Listeria monocytogenes can generate new actin structures in a vasodilator-stimulated phosphoprotein-dependent (VASP) manner, but independently of the Arp2/3 complex. These results are consistent with the concept that there are multiple actin-polymerization machines in cells. With these simple tests it is possible to probe the specific function of proteins or identify novel molecules that act upon cellular actin polymerization.