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dc.contributor.authorDamiano-Guercio, Julia
dc.contributor.authorKurzawa, Laëtitia
dc.contributor.authorMueller, Jan
dc.contributor.authorDimchev, Georgi
dc.contributor.authorSchaks, Matthias
dc.contributor.authorNemethova, Maria
dc.contributor.authorPokrant, Thomas
dc.contributor.authorBrühmann, Stefan
dc.contributor.authorLinkner, Joern
dc.contributor.authorBlanchoin, Laurent
dc.contributor.authorSixt, Michael
dc.contributor.authorRottner, Klemens
dc.contributor.authorFaix, Jan
dc.date.accessioned2020-12-03T14:57:11Z
dc.date.available2020-12-03T14:57:11Z
dc.date.issued2020-05-11
dc.identifier.citationElife. 2020 May 11;9:e55351. doi: 10.7554/eLife.55351.en_US
dc.identifier.pmid32391788
dc.identifier.doi10.7554/eLife.55351
dc.identifier.urihttp://hdl.handle.net/10033/622631
dc.description.abstractCell 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.en_US
dc.language.isoenen_US
dc.publishereLife Sciences Publicationsen_US
dc.rightsAttribution 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subjectEna/VASP proteinsen_US
dc.subjectcell adhesionen_US
dc.subjectcell biologyen_US
dc.subjectcell migrationen_US
dc.subjectfilopodiaen_US
dc.subjectlamellipodiaen_US
dc.subjectmicrospikesen_US
dc.subjectmouseen_US
dc.titleLoss of Ena/VASP interferes with lamellipodium architecture, motility and integrin-dependent adhesion.en_US
dc.typeArticleen_US
dc.identifier.eissn2050-084X
dc.contributor.departmentHZI,Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7,38124 Braunschweig, Germany.en_US
dc.identifier.journaleLifeen_US
dc.source.volume9
refterms.dateFOA2020-12-03T14:57:12Z
dc.source.journaltitleeLife
dc.source.countryEngland


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Attribution 4.0 International
Except where otherwise noted, this item's license is described as Attribution 4.0 International