Author response: Loss of Ena/VASP interferes with lamellipodium architecture, motility and integrin-dependent adhesion [peer_review]

Julia Damiano-Guercio, Laëtitia Kurzawa, Jan Mueller, Georgi Dimchev, Matthias Schaks, Maria Nemethova, Thomas Pokrant, Stefan Brühmann, Joern Linkner, Laurent Blanchoin, Michael Sixt, Klemens Rottner (+1 others)
2020 unpublished
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/Cas9mediated loss of Ena/VASP proteins reduced lamellipodial actin assembly and perturbed lamellipodial architecture, as
more » ... 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. Damiano-Guercio et al. eLife 2020;9:e55351.
doi:10.7554/elife.55351.sa2 fatcat:lwx65bb3v5cgzohgz2z3afrg4u