ActA and human zyxin harbour Arp2/3-independent actin-polymerization activity
Author: ["Julie Fradelizi","Vincent Noireaux","Julie Plastino","Bernadette Menichi","Daniel Louvard","Cécile Sykes","Roy M. Golsteyn","Evelyne Friederich"]
Publication: Nature Cell Biology
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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.
Cite this article
Fradelizi, J., Noireaux, V., Plastino, J. et al. ActA and human zyxin harbour Arp2/3-independent actin-polymerization activity. Nat Cell Biol 3, 699–707 (2001). https://doi.org/10.1038/35087009
