Reference : ActA and human zyxin harbour Arp2/3-independent actin-polymerization activity.
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
ActA and human zyxin harbour Arp2/3-independent actin-polymerization activity.
Fradelizi, J. [> >]
Noireaux, V. [> >]
Plastino, J. [> >]
Menichi, B. [> >]
Louvard, D. [> >]
Sykes, C. [> >]
Golsteyn, R. M. [> >]
Friederich, Evelyne mailto [University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit >]
Nature Cell Biology
Yes (verified by ORBilu)
[en] Actin Cytoskeleton/drug effects/metabolism/ultrastructure ; Actin-Related Protein 2 ; Actin-Related Protein 3 ; Actins/metabolism ; Animals ; Bacterial Proteins/metabolism ; Biological Assay ; Cell Adhesion Molecules/metabolism ; Cell-Free System ; Cercopithecus aethiops ; Cytoskeletal Proteins ; Fluorescent Antibody Technique ; Glycoproteins ; HeLa Cells/cytology/drug effects/metabolism ; Humans ; Membrane Proteins/metabolism ; Metalloproteins/genetics/metabolism ; Microfilament Proteins ; Microspheres ; Mitochondria/metabolism/ultrastructure ; Phosphoproteins/metabolism ; Polymers/metabolism ; Proteins/metabolism ; Recombinant Proteins/metabolism ; Transfection ; Vero Cells/cytology/drug effects/metabolism ; Wiskott-Aldrich Syndrome Protein ; Zyxin
[en] 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.

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