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Loss of Ena/VASP interferes with lamellipodium architecture, motility and integrin-dependent adhesion.
Damiano-Guercio, Julia Kurzawa, Laëtitia Mueller, Jan Dimchev, Georgi Schaks, Matthias Nemethova, Maria Pokrant, Thomas Brühmann, Stefan Linkner, Joern Blanchoin, Laurent
Damiano-Guercio, Julia
Kurzawa, Laëtitia
Mueller, Jan
Dimchev, Georgi
Schaks, Matthias
Nemethova, Maria
Pokrant, Thomas
Brühmann, Stefan
Linkner, Joern
Blanchoin, Laurent
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2020-05-11
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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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Elife. 2020 May 11;9:e55351. doi: 10.7554/eLife.55351.
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en
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2050-084X
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Attribution 4.0 International