埃希氏菌属肌动蛋白结合蛋白（ActA）和人类斑联蛋白具有不依赖于肌动蛋白相关蛋白2/3（Arp2/3）的肌动蛋白聚合活性。

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

作者信息

Fradelizi J, Noireaux V, Plastino J, Menichi B, Louvard D, Sykes C, Golsteyn R M, Friederich E

机构信息

Laboratoire de Morphogenèse et Signalisation Cellulaires, Unité Mixte de Recherche CNRS/Institut Curie (UMR144) 26 rue d'Ulm, 75248 Paris cedex 05, France.

出版信息

Nat Cell Biol. 2001 Aug;3(8):699-707. doi: 10.1038/35087009.

DOI:10.1038/35087009

PMID:11483954

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.

摘要

肌动蛋白细胞骨架是一个由多种F-肌动蛋白结构组成的动态网络。为了了解这些结构是如何产生的，我们在体外的珠子试验和细胞的线粒体靶向试验中测试了蛋白质指导肌动蛋白聚合的能力。我们发现人类桩蛋白和单核细胞增生李斯特菌的相关蛋白ActA可以以一种血管舒张刺激磷蛋白依赖性（VASP）的方式产生新的肌动蛋白结构，但独立于Arp2/3复合体。这些结果与细胞中存在多种肌动蛋白聚合机器的概念一致。通过这些简单的试验，可以探究蛋白质的特定功能或识别作用于细胞肌动蛋白聚合的新分子。