2.50
HDL Handle:
http://hdl.handle.net/10033/146010
Title:
Microtubules as platforms for assaying actin polymerization in vivo.
Authors:
Oelkers, J Margit; Vinzenz, Marlene; Nemethova, Maria; Jacob, Sonja; Lai, Frank P L; Block, Jennifer; Szczodrak, Malgorzata; Kerkhoff, Eugen; Backert, Steffen; Schlüter, Kai; Stradal, Theresia E B; Small, J Victor; Koestler, Stefan A; Rottner, Klemens
Abstract:
The 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.
Affiliation:
Helmholtz Centre for Infection Research, Braunschweig, Germany.
Citation:
Microtubules as platforms for assaying actin polymerization in vivo. 2011, 6 (5):e19931 PLoS ONE
Journal:
PloS one
Issue Date:
2011
URI:
http://hdl.handle.net/10033/146010
DOI:
10.1371/journal.pone.0019931
PubMed ID:
21603613
Type:
Article
Language:
en
ISSN:
1932-6203
Appears in Collections:
Publications of RG Signalling and Motility (SIM)

Full metadata record

DC FieldValueLanguage
dc.contributor.authorOelkers, J Margiten
dc.contributor.authorVinzenz, Marleneen
dc.contributor.authorNemethova, Mariaen
dc.contributor.authorJacob, Sonjaen
dc.contributor.authorLai, Frank P Len
dc.contributor.authorBlock, Jenniferen
dc.contributor.authorSzczodrak, Malgorzataen
dc.contributor.authorKerkhoff, Eugenen
dc.contributor.authorBackert, Steffenen
dc.contributor.authorSchlüter, Kaien
dc.contributor.authorStradal, Theresia E Ben
dc.contributor.authorSmall, J Victoren
dc.contributor.authorKoestler, Stefan Aen
dc.contributor.authorRottner, Klemensen
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.en
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

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