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dc.contributor.authorOelkers, J Margit
dc.contributor.authorVinzenz, Marlene
dc.contributor.authorNemethova, Maria
dc.contributor.authorJacob, Sonja
dc.contributor.authorLai, Frank P L
dc.contributor.authorBlock, Jennifer
dc.contributor.authorSzczodrak, Malgorzata
dc.contributor.authorKerkhoff, Eugen
dc.contributor.authorBackert, Steffen
dc.contributor.authorSchlüter, Kai
dc.contributor.authorStradal, Theresia E B
dc.contributor.authorSmall, J Victor
dc.contributor.authorKoestler, Stefan A
dc.contributor.authorRottner, Klemens
dc.date.accessioned2011-10-19T13:44:11Z
dc.date.available2011-10-19T13:44:11Z
dc.date.issued2011
dc.identifier.citationMicrotubules as platforms for assaying actin polymerization in vivo. 2011, 6 (5):e19931 PLoS ONEen
dc.identifier.issn1932-6203
dc.identifier.pmid21603613
dc.identifier.doi10.1371/journal.pone.0019931
dc.identifier.urihttp://hdl.handle.net/10033/146010
dc.description.abstractThe actin cytoskeleton is continuously remodeled through cycles of actin filament assembly and disassembly. Filaments are born through nucleation and shaped into supramolecular structures with various essential functions. These range from contractile and protrusive assemblies in muscle and non-muscle cells to actin filament comets propelling vesicles or pathogens through the cytosol. Although nucleation has been extensively studied using purified proteins in vitro, dissection of the process in cells is complicated by the abundance and molecular complexity of actin filament arrays. We here describe the ectopic nucleation of actin filaments on the surface of microtubules, free of endogenous actin and interfering membrane or lipid. All major mechanisms of actin filament nucleation were recapitulated, including filament assembly induced by Arp2/3 complex, formin and Spir. This novel approach allows systematic dissection of actin nucleation in the cytosol of live cells, its genetic re-engineering as well as screening for new modifiers of the process.
dc.language.isoenen
dc.titleMicrotubules as platforms for assaying actin polymerization in vivo.en
dc.typeArticleen
dc.contributor.departmentHelmholtz Centre for Infection Research, Braunschweig, Germany.en
dc.identifier.journalPloS oneen
refterms.dateFOA2018-06-12T23:42:40Z
html.description.abstractThe actin cytoskeleton is continuously remodeled through cycles of actin filament assembly and disassembly. Filaments are born through nucleation and shaped into supramolecular structures with various essential functions. These range from contractile and protrusive assemblies in muscle and non-muscle cells to actin filament comets propelling vesicles or pathogens through the cytosol. Although nucleation has been extensively studied using purified proteins in vitro, dissection of the process in cells is complicated by the abundance and molecular complexity of actin filament arrays. We here describe the ectopic nucleation of actin filaments on the surface of microtubules, free of endogenous actin and interfering membrane or lipid. All major mechanisms of actin filament nucleation were recapitulated, including filament assembly induced by Arp2/3 complex, formin and Spir. This novel approach allows systematic dissection of actin nucleation in the cytosol of live cells, its genetic re-engineering as well as screening for new modifiers of the process.


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