Ena/VASP Proteins Cooperate with the WAVE Complex to Regulate the Actin Cytoskeleton

被引：88

作者：

Chen, Xing Judy ^{[1
]}

Squarr, Anna Julia ^{[2
]}

Stephan, Raiko ^{[2
]}

Chen, Baoyu ^{[3
,4
]}

Higgins, Theresa E. ^{[1
]}

Barry, David J. ^{[1
]}

Martin, Morag C. ^{[1
]}

Rosen, Michael K. ^{[3
,4
]}

Bogdan, Sven ^{[2
]}

Way, Michael ^{[1
]}

机构：

[1] Canc Res UK, London Res Inst, Cell Motil Lab, London WC2A 3LY, England

[2] Univ Munster, Inst Neurobiol, D-48149 Munster, Germany

[3] Univ Texas SW Med Ctr Dallas, Howard Hughes Med Inst, Dallas, TX 75390 USA

[4] Univ Texas SW Med Ctr Dallas, Dept Biophys, Dallas, TX 75390 USA

来源：

DEVELOPMENTAL CELL | 2014年 / 30卷 / 05期

关键词：

ABL TYROSINE KINASE; STIMULATED PHOSPHOPROTEIN; EVH1; DOMAIN; DROSOPHILA; RECOGNITION; LIGAND; WASP; VASP; SUBSTRATE; MEMBRANE;

D O I：

10.1016/j.devcel.2014.08.001

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Ena/VASP proteins and the WAVE regulatory complex (WRC) regulate cell motility by virtue of their ability to independently promote actin polymerization. We demonstrate that Ena/VASP and the WRC control actin polymerization in a cooperative manner through the interaction of the Ena/VASP EVH1 domain with an extended proline rich motif in Abi. This interaction increases cell migration and enables VASP to cooperatively enhance WRC stimulation of Arp2/3 complex-mediated actin assembly in vitro in the presence of Rac. Loss of this interaction in Drosophila macrophages results in defects in lamel-lipodia formation, cell spreading, and redistribution of Ena to the tips of filopodia-like extensions. Rescue experiments of abi mutants also reveals a physiological requirement for the Abi: Ena interaction in photoreceptor axon targeting and oogenesis. Our data demonstrate that the activities of Ena/VASP and the WRC are intimately linked to ensure optimal control of actin polymerization during cell migration and development.

引用

页码：569 / 584

页数：16

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