AI Article Synopsis
- Ena/VASP proteins and the WAVE regulatory complex (WRC) work together to enhance actin polymerization, which is crucial for cell motility.
- Their interaction, specifically between the Ena/VASP EVH1 domain and a proline-rich motif in Abi, boosts cell migration by promoting Arp2/3 complex-mediated actin assembly when Rac is present.
- Disruption of this interaction in Drosophila macrophages leads to impaired lamellipodia formation and other developmental defects, highlighting the importance of the Ena-Abi partnership in cellular processes like axon targeting and oogenesis.
Article 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 in vitro in the 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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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4165403 | PMC |
| http://dx.doi.org/10.1016/j.devcel.2014.08.001 | DOI Listing |
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