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WAVE binds Ena/VASP for enhanced Arp2/3 complex–based actin assembly
The WAVE complex is the main activator of the Arp2/3 complex for actin filament nucleation and assembly in the lamellipodia of moving cells. Other important players in lamellipodial protrusion are Ena/VASP proteins, which enhance actin filament elongation. Here we examine the molecular coordination...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4279229/ https://www.ncbi.nlm.nih.gov/pubmed/25355952 http://dx.doi.org/10.1091/mbc.E14-07-1200 |
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author | Havrylenko, Svitlana Noguera, Philippe Abou-Ghali, Majdouline Manzi, John Faqir, Fahima Lamora, Audrey Guérin, Christophe Blanchoin, Laurent Plastino, Julie |
author_facet | Havrylenko, Svitlana Noguera, Philippe Abou-Ghali, Majdouline Manzi, John Faqir, Fahima Lamora, Audrey Guérin, Christophe Blanchoin, Laurent Plastino, Julie |
author_sort | Havrylenko, Svitlana |
collection | PubMed |
description | The WAVE complex is the main activator of the Arp2/3 complex for actin filament nucleation and assembly in the lamellipodia of moving cells. Other important players in lamellipodial protrusion are Ena/VASP proteins, which enhance actin filament elongation. Here we examine the molecular coordination between the nucleating activity of the Arp2/3 complex and the elongating activity of Ena/VASP proteins for the formation of actin networks. Using an in vitro bead motility assay, we show that WAVE directly binds VASP, resulting in an increase in Arp2/3 complex–based actin assembly. We show that this interaction is important in vivo as well, for the formation of lamellipodia during the ventral enclosure event of Caenorhabditis elegans embryogenesis. Ena/VASP's ability to bind F-actin and profilin-complexed G-actin are important for its effect, whereas Ena/VASP tetramerization is not necessary. Our data are consistent with the idea that binding of Ena/VASP to WAVE potentiates Arp2/3 complex activity and lamellipodial actin assembly. |
format | Online Article Text |
id | pubmed-4279229 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-42792292015-03-16 WAVE binds Ena/VASP for enhanced Arp2/3 complex–based actin assembly Havrylenko, Svitlana Noguera, Philippe Abou-Ghali, Majdouline Manzi, John Faqir, Fahima Lamora, Audrey Guérin, Christophe Blanchoin, Laurent Plastino, Julie Mol Biol Cell Articles The WAVE complex is the main activator of the Arp2/3 complex for actin filament nucleation and assembly in the lamellipodia of moving cells. Other important players in lamellipodial protrusion are Ena/VASP proteins, which enhance actin filament elongation. Here we examine the molecular coordination between the nucleating activity of the Arp2/3 complex and the elongating activity of Ena/VASP proteins for the formation of actin networks. Using an in vitro bead motility assay, we show that WAVE directly binds VASP, resulting in an increase in Arp2/3 complex–based actin assembly. We show that this interaction is important in vivo as well, for the formation of lamellipodia during the ventral enclosure event of Caenorhabditis elegans embryogenesis. Ena/VASP's ability to bind F-actin and profilin-complexed G-actin are important for its effect, whereas Ena/VASP tetramerization is not necessary. Our data are consistent with the idea that binding of Ena/VASP to WAVE potentiates Arp2/3 complex activity and lamellipodial actin assembly. The American Society for Cell Biology 2015-01-01 /pmc/articles/PMC4279229/ /pubmed/25355952 http://dx.doi.org/10.1091/mbc.E14-07-1200 Text en © 2015 Havrylenko, Noguera, et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. |
spellingShingle | Articles Havrylenko, Svitlana Noguera, Philippe Abou-Ghali, Majdouline Manzi, John Faqir, Fahima Lamora, Audrey Guérin, Christophe Blanchoin, Laurent Plastino, Julie WAVE binds Ena/VASP for enhanced Arp2/3 complex–based actin assembly |
title | WAVE binds Ena/VASP for enhanced Arp2/3 complex–based actin assembly |
title_full | WAVE binds Ena/VASP for enhanced Arp2/3 complex–based actin assembly |
title_fullStr | WAVE binds Ena/VASP for enhanced Arp2/3 complex–based actin assembly |
title_full_unstemmed | WAVE binds Ena/VASP for enhanced Arp2/3 complex–based actin assembly |
title_short | WAVE binds Ena/VASP for enhanced Arp2/3 complex–based actin assembly |
title_sort | wave binds ena/vasp for enhanced arp2/3 complex–based actin assembly |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4279229/ https://www.ncbi.nlm.nih.gov/pubmed/25355952 http://dx.doi.org/10.1091/mbc.E14-07-1200 |
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