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dc.contributor.authorEgile, C
dc.contributor.authorRouiller, I
dc.contributor.authorXu, XP
dc.contributor.authorVolkmann, N
dc.contributor.authorLi, R
dc.contributor.authorHanein, D
dc.date.accessioned2020-12-09T23:24:01Z
dc.date.available2020-12-09T23:24:01Z
dc.date.issued2005-11-01
dc.identifierpii: 05-PLBI-RA-0520R2
dc.identifier.citationEgile, C., Rouiller, I., Xu, X. P., Volkmann, N., Li, R. & Hanein, D. (2005). Mechanism of filament nucleation and branch stability revealed by the structure of the Arp2/3 complex at actin branch junctions. PLOS BIOLOGY, 3 (11), pp.1902-1909. https://doi.org/10.1371/journal.pbio.0030383.
dc.identifier.issn1545-7885
dc.identifier.urihttp://hdl.handle.net/11343/253212
dc.description.abstractActin branch junctions are conserved cytoskeletal elements critical for the generation of protrusive force during actin polymerization-driven cellular motility. Assembly of actin branch junctions requires the Arp2/3 complex, upon activation, to initiate a new actin (daughter) filament branch from the side of an existing (mother) filament, leading to the formation of a dendritic actin network with the fast growing (barbed) ends facing the direction of movement. Using genetic labeling and electron microscopy, we have determined the structural organization of actin branch junctions assembled in vitro with 1-nm precision. We show here that the activators of the Arp2/3 complex, except cortactin, dissociate after branch formation. The Arp2/3 complex associates with the mother filament through a comprehensive network of interactions, with the long axis of the complex aligned nearly perpendicular to the mother filament. The actin-related proteins, Arp2 and Arp3, are positioned with their barbed ends facing the direction of daughter filament growth. This subunit map brings direct structural insights into the mechanism of assembly and mechanical stability of actin branch junctions.
dc.languageEnglish
dc.publisherPUBLIC LIBRARY SCIENCE
dc.rights.urihttps://creativecommons.org/licenses/by/4.0
dc.titleMechanism of filament nucleation and branch stability revealed by the structure of the Arp2/3 complex at actin branch junctions
dc.typeJournal Article
dc.identifier.doi10.1371/journal.pbio.0030383
melbourne.affiliation.departmentBiochemistry and Molecular Biology
melbourne.source.titlePLoS Biology
melbourne.source.volume3
melbourne.source.issue11
melbourne.source.pages1902-1909
dc.rights.licenseCC BY
melbourne.elementsid1308559
melbourne.contributor.authorRouiller, Isabelle
dc.identifier.eissn1545-7885
melbourne.accessrightsOpen Access


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