Ena/VASP proteins cooperate with the WAVE complex to regulate the actin cytoskeleton

Xing Judy Chen; Anna Julia Squarr; Raiko Stephan; Baoyu Chen; Theresa E. Higgins; David J. Barry; Morag C. Martin; Michael K. Rosen; Sven Bogdan; Michael Way

doi:10.1016/j.devcel.2014.08.001

Ena/VASP proteins cooperate with the WAVE complex to regulate the actin cytoskeleton

Xing Judy Chen, Anna Julia Squarr, Raiko Stephan, Baoyu Chen, Theresa E. Higgins, David J. Barry, Morag C. Martin, Michael K. Rosen, Sven Bogdan, Michael Way

Research output: Contribution to journal › Article › peer-review

81 Scopus citations

Abstract

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 invitro inthe presence of Rac. Loss of this interaction in Drosophila macrophages results in defects in lamellipodia 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.

Original language	English (US)
Pages (from-to)	569-584
Number of pages	16
Journal	Developmental cell
Volume	30
Issue number	5
DOIs	https://doi.org/10.1016/j.devcel.2014.08.001
State	Published - Sep 8 2014

ASJC Scopus subject areas

Molecular Biology
General Biochemistry, Genetics and Molecular Biology
Developmental Biology
Cell Biology

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title = "Ena/VASP proteins cooperate with the WAVE complex to regulate the actin cytoskeleton",

abstract = "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 invitro inthe presence of Rac. Loss of this interaction in Drosophila macrophages results in defects in lamellipodia 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.",

author = "Chen, {Xing Judy} and Squarr, {Anna Julia} and Raiko Stephan and Baoyu Chen and Higgins, {Theresa E.} and Barry, {David J.} and Martin, {Morag C.} and Rosen, {Michael K.} and Sven Bogdan and Michael Way",

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doi = "10.1016/j.devcel.2014.08.001",

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AU - Chen, Xing Judy

AU - Squarr, Anna Julia

AU - Stephan, Raiko

AU - Chen, Baoyu

AU - Higgins, Theresa E.

AU - Barry, David J.

AU - Martin, Morag C.

AU - Rosen, Michael K.

AU - Bogdan, Sven

AU - Way, Michael

PY - 2014/9/8

Y1 - 2014/9/8

N2 - 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 invitro inthe presence of Rac. Loss of this interaction in Drosophila macrophages results in defects in lamellipodia 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.

AB - 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 invitro inthe presence of Rac. Loss of this interaction in Drosophila macrophages results in defects in lamellipodia 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.

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Ena/VASP proteins cooperate with the WAVE complex to regulate the actin cytoskeleton

Abstract

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