ActA and human zyxin harbour Arp2/3-independent actin-polymerization activity

被引:99
作者
Fradelizi, J
Noireaux, V
Plastino, J
Menichi, B
Louvard, D
Sykes, C
Golsteyn, RM
Friederich, E
机构
[1] Inst Curie, Lab Morphogenese & Signalisat Cellulaires, CNRS, UMR 144, F-75248 Paris 05, France
[2] Inst Curie, Lab Physicochim Curie, CNRS, UMR 168, F-75248 Paris, France
[3] Ctr Univ, CRP Sante, CNRS, Lab Franco Luxembourgeois Rech Biomed, L-1511 Luxembourg, Luxembourg
关键词
D O I
10.1038/35087009
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
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.
引用
收藏
页码:699 / 707
页数:9
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