[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.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Fradelizi, J.
Noireaux, V.
Plastino, J.
Menichi, B.
Louvard, D.
Sykes, C.
Golsteyn, R. M.
FRIEDERICH, Evelyne ; University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit
Language :
English
Title :
ActA and human zyxin harbour Arp2/3-independent actin-polymerization activity.
