AI Article Synopsis
- Cell migration relies on actin structures like lamellipodia and filopodia, along with focal adhesions, to facilitate movement; however, Ena/VASP proteins, previously thought to hinder this process, actually enhance it in mouse cell lines.
- The study found that removing Ena/VASP proteins using CRISPR/Cas9 led to less actin assembly in lamellipodia and altered their structure, affecting the geometry and reducing filament numbers and lengths.
- Ena/VASP loss also disrupted microspike formation, impaired integrin-mediated adhesion, and decreased traction forces, indicating these proteins play an essential role in promoting cell migration.
Article Abstract
Cell migration entails networks and bundles of actin filaments termed lamellipodia and microspikes or filopodia, respectively, as well as focal adhesions, all of which recruit Ena/VASP family members hitherto thought to antagonize efficient cell motility. However, we find these proteins to act as positive regulators of migration in different murine cell lines. CRISPR/Cas9-mediated loss of Ena/VASP proteins reduced lamellipodial actin assembly and perturbed lamellipodial architecture, as evidenced by changed network geometry as well as reduction of filament length and number that was accompanied by abnormal Arp2/3 complex and heterodimeric capping protein accumulation. Loss of Ena/VASP function also abolished the formation of microspikes normally embedded in lamellipodia, but not of filopodia capable of emanating without lamellipodia. Ena/VASP-deficiency also impaired integrin-mediated adhesion accompanied by reduced traction forces exerted through these structures. Our data thus uncover novel Ena/VASP functions of these actin polymerases that are fully consistent with their promotion of cell migration.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7239657 | PMC |
| http://dx.doi.org/10.7554/eLife.55351 | DOI Listing |
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