Loss of Ena/VASP interferes with lamellipodium architecture, motility and integrin-dependent adhesion - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue eLife Année : 2020

Loss of Ena/VASP interferes with lamellipodium architecture, motility and integrin-dependent adhesion

Résumé

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.
Fichier principal
Vignette du fichier
Damiano et al.pdf (10.05 Mo) Télécharger le fichier
Origine : Fichiers éditeurs autorisés sur une archive ouverte
Loading...

Dates et versions

hal-02777207 , version 1 (09-10-2020)

Licence

Paternité

Identifiants

Citer

Julia Damiano-Guercio, Laetitia Kurzawa, Jan Mueller, Georgi Dimchev, Matthias Schaks, et al.. Loss of Ena/VASP interferes with lamellipodium architecture, motility and integrin-dependent adhesion. eLife, 2020, 9, ⟨10.7554/eLife.55351⟩. ⟨hal-02777207⟩
86 Consultations
58 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More