{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T20:13:20Z","timestamp":1791317600173,"version":"4.3.1"},"reference-count":70,"publisher":"eLife Sciences Publications, Ltd","license":[{"start":{"date-parts":[[2013,9,3]],"date-time":"2013-09-03T00:00:00Z","timestamp":1378166400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/3.0\/"},{"start":{"date-parts":[[2013,9,3]],"date-time":"2013-09-03T00:00:00Z","timestamp":1378166400000},"content-version":"am","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/3.0\/"},{"start":{"date-parts":[[2013,9,3]],"date-time":"2013-09-03T00:00:00Z","timestamp":1378166400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/3.0\/"},{"start":{"date-parts":[[2013,9,3]],"date-time":"2013-09-03T00:00:00Z","timestamp":1378166400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/3.0\/"},{"start":{"date-parts":[[2013,9,3]],"date-time":"2013-09-03T00:00:00Z","timestamp":1378166400000},"content-version":"am","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/3.0\/"},{"start":{"date-parts":[[2013,9,3]],"date-time":"2013-09-03T00:00:00Z","timestamp":1378166400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/3.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["GM43369"],"award-info":[{"award-number":["GM43369"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000011","name":"Howard Hughes Medical Institute","doi-asserted-by":"crossref","id":[{"id":"10.13039\/100000011","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000928","name":"Welch Foundation","doi-asserted-by":"crossref","award":["I-1544"],"award-info":[{"award-number":["I-1544"]}],"id":[{"id":"10.13039\/100000928","id-type":"DOI","asserted-by":"crossref"}]},{"name":"National Science Foundation","award":["MRSEC 0820492"],"award-info":[{"award-number":["MRSEC 0820492"]}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["GM56322"],"award-info":[{"award-number":["GM56322"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["GM63691"],"award-info":[{"award-number":["GM63691"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["GM098143"],"award-info":[{"award-number":["GM098143"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["GM43369"],"award-info":[{"award-number":["GM43369"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000011","name":"Howard Hughes Medical Institute","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000011","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000928","name":"Welch Foundation","doi-asserted-by":"publisher","award":["I-1544"],"award-info":[{"award-number":["I-1544"]}],"id":[{"id":"10.13039\/100000928","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000001","name":"National Science Foundation","doi-asserted-by":"publisher","award":["MRSEC 0820492"],"award-info":[{"award-number":["MRSEC 0820492"]}],"id":[{"id":"10.13039\/100000001","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["GM56322"],"award-info":[{"award-number":["GM56322"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["GM63691"],"award-info":[{"award-number":["GM63691"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["GM098143"],"award-info":[{"award-number":["GM098143"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.elifesciences.org"],"crossmark-restriction":false},"short-container-title":[],"abstract":"<jats:p>During cell locomotion and endocytosis, membrane-tethered WASP proteins stimulate actin filament nucleation by the Arp2\/3 complex. This process generates highly branched arrays of filaments that grow toward the membrane to which they are tethered, a conflict that seemingly would restrict filament growth. Using three-color single-molecule imaging in vitro we revealed how the dynamic associations of Arp2\/3 complex with mother filament and WASP are temporally coordinated with initiation of daughter filament growth. We found that WASP proteins dissociated from filament-bound Arp2\/3 complex prior to new filament growth. Further, mutations that accelerated release of WASP from filament-bound Arp2\/3 complex proportionally accelerated branch formation. These data suggest that while WASP promotes formation of pre-nucleation complexes, filament growth cannot occur until it is triggered by WASP release. This provides a mechanism by which membrane-bound WASP proteins can stimulate network growth without restraining it.<\/jats:p>","DOI":"10.7554\/elife.01008","type":"journal-article","created":{"date-parts":[[2013,9,4]],"date-time":"2013-09-04T11:38:51Z","timestamp":1378294731000},"source":"Crossref","is-referenced-by-count":120,"title":["Three-color single molecule imaging shows WASP detachment from Arp2\/3 complex triggers actin filament branch formation"],"prefix":"10.7554","volume":"2","author":[{"given":"Benjamin A","family":"Smith","sequence":"first","affiliation":[{"name":"Department of Biochemistry, Brandeis University, Waltham, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shae B","family":"Padrick","sequence":"additional","affiliation":[{"name":"Department of Biophysics, Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lynda K","family":"Doolittle","sequence":"additional","affiliation":[{"name":"Department of Biophysics, Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karen","family":"Daugherty-Clarke","sequence":"additional","affiliation":[{"name":"Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, United States"},{"name":"Department of Biology, Brandeis University, Waltham, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"suffix":"Jr","given":"Ivan R","family":"Corr\u00eaa","sequence":"additional","affiliation":[{"name":"New England Biolabs, Ipswich, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ming-Qun","family":"Xu","sequence":"additional","affiliation":[{"name":"New England Biolabs, Ipswich, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bruce L","family":"Goode","sequence":"additional","affiliation":[{"name":"Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, United States"},{"name":"Department of Biology, Brandeis University, Waltham, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael K","family":"Rosen","sequence":"additional","affiliation":[{"name":"Department of Biophysics, Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jeff","family":"Gelles","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Brandeis University, Waltham, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"4374","published-online":{"date-parts":[[2013,9,3]]},"reference":[{"key":"bib1","doi-asserted-by":"publisher","first-page":"423","DOI":"10.1016\/j.cub.2009.12.056","article-title":"A \u2018primer\u2019-based mechanism underlies branched actin filament network formation and motility","volume":"20","author":"Achard","year":"2010","journal-title":"Curr Biol"},{"key":"bib2","doi-asserted-by":"publisher","first-page":"15009","DOI":"10.1073\/pnas.211556398","article-title":"Direct real-time observation of actin filament branching mediated by Arp2\/3 complex using total internal reflection fluorescence microscopy","volume":"98","author":"Amann","year":"2001","journal-title":"Proc Natl Acad Sci USA"},{"key":"bib3","doi-asserted-by":"publisher","first-page":"1450","DOI":"10.1016\/j.cub.2011.07.046","article-title":"Distinct roles for f-bar proteins Cdc15p and Bzz1p in actin polymerization at sites of endocytosis in fission yeast","volume":"21","author":"Arasada","year":"2011","journal-title":"Curr Biol"},{"key":"bib4","doi-asserted-by":"publisher","first-page":"7135","DOI":"10.1074\/jbc.M705894200","article-title":"Pathway of actin filament branch formation by Arp2\/3 complex","volume":"283","author":"Beltzner","year":"2008","journal-title":"J Biol Chem"},{"key":"bib5","doi-asserted-by":"publisher","first-page":"1007","DOI":"10.1038\/35010008","article-title":"Direct observation of dendritic actin filament networks nucleated by Arp2\/3 complex and WASP\/Scar proteins","volume":"404","author":"Blanchoin","year":"2000","journal-title":"Nature"},{"key":"bib6","doi-asserted-by":"publisher","first-page":"695","DOI":"10.1016\/j.str.2008.02.013","article-title":"X-ray scattering study of activated Arp2\/3 complex with bound actin-WCA","volume":"16","author":"Boczkowska","year":"2008","journal-title":"Structure"},{"key":"bib7","doi-asserted-by":"publisher","first-page":"237","DOI":"10.1038\/nrm2867","article-title":"A nucleator arms race: cellular control of actin assembly","volume":"11","author":"Campellone","year":"2010","journal-title":"Nat Rev Mol Cell Biol"},{"key":"bib8","doi-asserted-by":"publisher","first-page":"16644","DOI":"10.1073\/pnas.0507021102","article-title":"Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly","volume":"102","author":"Chereau","year":"2005","journal-title":"Proc Natl Acad Sci USA"},{"key":"bib9","doi-asserted-by":"publisher","first-page":"901","DOI":"10.1016\/j.cell.2006.12.049","article-title":"Mechanism of actin network attachment to moving membranes: barbed end capture by N-WASP WH2 domains","volume":"128","author":"Co","year":"2007","journal-title":"Cell"},{"key":"bib10","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1007\/BF00712034","article-title":"Pyrene actin: documentation of the validity of a sensitive assay for actin polymerization","volume":"4","author":"Cooper","year":"1983","journal-title":"J Muscle Res Cell Motil"},{"key":"bib11","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1006\/jcis.1996.0217","article-title":"Methods of digital video microscopy for colloidal studies","volume":"179","author":"Crocker","year":"1996","journal-title":"J Colloid Interface Sci"},{"key":"bib12","doi-asserted-by":"publisher","first-page":"35","DOI":"10.1534\/genetics.105.040634","article-title":"Dissection of Arp2\/3 complex actin nucleation mechanism and distinct roles for its nucleation-promoting factors in Saccharomyces cerevisiae","volume":"171","author":"D\u2019Agostino","year":"2005","journal-title":"Genetics"},{"key":"bib13","doi-asserted-by":"publisher","first-page":"14871","DOI":"10.1073\/pnas.261419298","article-title":"Arp2\/3 complex requires hydrolyzable ATP for nucleation of new actin filaments","volume":"98","author":"Dayel","year":"2001","journal-title":"Proc Natl Acad Sci USA"},{"key":"bib14","doi-asserted-by":"publisher","first-page":"E91","DOI":"10.1371\/journal.pbio.0020091","article-title":"Activation of Arp2\/3 complex: addition of the first subunit of the new filament by a WASP protein triggers rapid ATP hydrolysis on Arp2","volume":"2","author":"Dayel","year":"2004","journal-title":"PLOS Biol"},{"key":"bib15","doi-asserted-by":"publisher","first-page":"643","DOI":"10.1083\/jcb.201111113","article-title":"Stoichiometry of Nck-dependent actin polymerization in living cells","volume":"197","author":"Ditlev","year":"2012","journal-title":"J Cell biol"},{"key":"bib16","doi-asserted-by":"publisher","first-page":"273","DOI":"10.1007\/978-1-62703-538-5_16","article-title":"Measurement and analysis of in vitro actin polymerization","volume":"1046","author":"Doolittle","year":"2013a","journal-title":"Methods Mol Biol"},{"key":"bib17","doi-asserted-by":"publisher","first-page":"251","DOI":"10.1007\/978-1-62703-538-5_15","article-title":"Purification of Arp2\/3 complex from Saccharomyces cerevisiae","volume":"1046","author":"Doolittle","year":"2013b","journal-title":"Methods Mol Biol"},{"key":"bib18","doi-asserted-by":"publisher","first-page":"231","DOI":"10.1007\/978-1-62703-538-5_14","article-title":"Purification of native Arp2\/3 complex from bovine thymus","volume":"1046","author":"Doolittle","year":"2013c","journal-title":"Methods Mol Biol"},{"key":"bib19","doi-asserted-by":"publisher","first-page":"1319","DOI":"10.1083\/jcb.146.6.1319","article-title":"Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2\/3 complex and bacterial actin-based motility","volume":"146","author":"Egile","year":"1999","journal-title":"J Cell Biol"},{"key":"bib20","doi-asserted-by":"publisher","first-page":"e383","DOI":"10.1371\/journal.pbio.0030383","article-title":"Mechanism of filament nucleation and branch stability revealed by the structure of the Arp2\/3 complex at actin branch junctions","volume":"3","author":"Egile","year":"2005","journal-title":"PLOS Biol"},{"key":"bib21","doi-asserted-by":"publisher","first-page":"23852","DOI":"10.1074\/jbc.M803448200","article-title":"Close packing of Listeria monocytogenes ActA, a natively unfolded protein, enhances F-actin assembly without dimerization","volume":"283","author":"Footer","year":"2008","journal-title":"J Biol Chem"},{"key":"bib22","doi-asserted-by":"publisher","first-page":"1023","DOI":"10.1529\/biophysj.106.084004","article-title":"Viewing dynamic assembly of molecular complexes by multi-wavelength single-molecule fluorescence","volume":"91","author":"Friedman","year":"2006","journal-title":"Biophys J"},{"key":"bib23","doi-asserted-by":"publisher","first-page":"679","DOI":"10.1016\/j.cell.2012.01.018","article-title":"Mechanism of transcription initiation at an activator-dependent promoter defined by single-molecule observation","volume":"148","author":"Friedman","year":"2012","journal-title":"Cell"},{"key":"bib24","doi-asserted-by":"publisher","first-page":"269","DOI":"10.1016\/j.molcel.2004.09.018","article-title":"Critical conformational changes in the Arp2\/3 complex are induced by nucleotide and nucleation promoting factor","volume":"16","author":"Goley","year":"2004","journal-title":"Mol Cell"},{"key":"bib25","doi-asserted-by":"publisher","first-page":"e00884","DOI":"10.7554\/eLife.00884","article-title":"Mechanism of synergistic activation of Arp2\/3 complex by cortactin and N-WASP","volume":"2","author":"Helgeson","year":"2013","journal-title":"eLife"},{"key":"bib26","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1016\/S0092-8674(04)00403-9","article-title":"The beta-thymosin\/WH2 domain; structural basis for the switch from inhibition to promotion of actin assembly","volume":"117","author":"Hertzog","year":"2004","journal-title":"Cell"},{"key":"bib27","doi-asserted-by":"publisher","first-page":"701","DOI":"10.1016\/j.chembiol.2013.03.019","article-title":"Small molecules CK-666 and CK-869 inhibit actin-related protein 2\/3 complex by blocking an activating conformational change","volume":"20","author":"Hetrick","year":"2013","journal-title":"Chem Biol"},{"key":"bib28","doi-asserted-by":"crossref","first-page":"15212","DOI":"10.1021\/bi991843+","article-title":"Influence of the C terminus of Wiskott-Aldrich syndrome protein (WASp) and the Arp2\/3 complex on actin polymerization","volume":"38","author":"Higgs","year":"1999","journal-title":"Biochemistry"},{"key":"bib29","doi-asserted-by":"publisher","first-page":"1289","DOI":"10.1126\/science.1198830","article-title":"Ordered and dynamic assembly of single spliceosomes","volume":"331","author":"Hoskins","year":"2011","journal-title":"Science"},{"key":"bib30","doi-asserted-by":"publisher","first-page":"619","DOI":"10.1083\/jcb.201211069","article-title":"Arp2\/3 complex ATP hydrolysis promotes lamellipodial actin network disassembly but is dispensable for assembly","volume":"200","author":"Ingerman","year":"2013","journal-title":"J Cell Biol"},{"key":"bib31","doi-asserted-by":"publisher","first-page":"3599","DOI":"10.1038\/sj.emboj.7600372","article-title":"Structural basis of actin sequestration by thymosin-\u00df4: implications for WH2 proteins","volume":"23","author":"Irobi","year":"2004","journal-title":"EMBO J"},{"key":"bib32","doi-asserted-by":"publisher","first-page":"11554","DOI":"10.1021\/bi048899a","article-title":"Expression of a nonpolymerizable actin mutant in Sf9 cells","volume":"43","author":"Joel","year":"2004","journal-title":"Biochemistry"},{"key":"bib33","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1016\/S0092-8674(03)00883-3","article-title":"A pathway for association of receptors, adaptors, and actin during endocytic internalization","volume":"115","author":"Kaksonen","year":"2003","journal-title":"Cell"},{"key":"bib34","doi-asserted-by":"publisher","first-page":"9955","DOI":"10.1073\/pnas.0401923101","article-title":"Labeling of fusion proteins with synthetic fluorophores in live cells","volume":"101","author":"Keppler","year":"2004","journal-title":"Proc Natl Acad Sci USA"},{"key":"bib35","doi-asserted-by":"publisher","first-page":"2725","DOI":"10.1016\/j.bmcl.2004.03.078","article-title":"Synthesis and characterization of bifunctional probes for the specific labeling of fusion proteins","volume":"14","author":"Kindermann","year":"2004","journal-title":"Bioorg Med Chem Lett"},{"key":"bib36","doi-asserted-by":"publisher","first-page":"982","DOI":"10.1038\/emboj.2008.34","article-title":"Arp2\/3 complex interactions and actin network turnover in lamellipodia","volume":"27","author":"Lai","year":"2008","journal-title":"EMBO J"},{"key":"bib37","doi-asserted-by":"publisher","first-page":"261","DOI":"10.1083\/jcb.200104094","article-title":"A two-tiered mechanism by which Cdc42 controls the localization and activation of an Arp2\/3-activating motor complex in yeast","volume":"155","author":"Lechler","year":"2001","journal-title":"J Cell Biol"},{"key":"bib38","doi-asserted-by":"publisher","first-page":"613","DOI":"10.1038\/44183","article-title":"Reconstitution of actin-based motility of Listeria and Shigella using pure proteins","volume":"401","author":"Loisel","year":"1999","journal-title":"Nature"},{"key":"bib39","doi-asserted-by":"publisher","first-page":"3739","DOI":"10.1073\/pnas.96.7.3739","article-title":"Scar, a WASp-related protein, activates nucleation of actin filaments by the Arp2\/3 complex","volume":"96","author":"Machesky","year":"1999","journal-title":"Proc Natl Acad Sci USA"},{"key":"bib40","doi-asserted-by":"publisher","first-page":"1347","DOI":"10.1016\/S0960-9822(98)00015-3","article-title":"Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2\/3 complex","volume":"8","author":"Machesky","year":"1998","journal-title":"Curr Biol"},{"key":"bib41","doi-asserted-by":"publisher","first-page":"76","DOI":"10.1038\/35050590","article-title":"Interaction of WASP\/Scar proteins with actin and vertebrate Arp2\/3 complex","volume":"3","author":"Marchand","year":"2001","journal-title":"Nat Cell Biol"},{"key":"bib42","doi-asserted-by":"publisher","first-page":"826","DOI":"10.1038\/ncb1443","article-title":"Arp2\/3 ATP hydrolysis-catalysed branch dissociation is critical for endocytic force generation","volume":"8","author":"Martin","year":"2006","journal-title":"Nat Cell Biol"},{"key":"bib43","doi-asserted-by":"publisher","first-page":"73","DOI":"10.1006\/bbrc.1997.8064","article-title":"Direct binding of the verprolin-homology domain in N-WASP to actin is essential for cytoskeletal reorganization","volume":"243","author":"Miki","year":"1998","journal-title":"Biochem Biophys Res Commun"},{"key":"bib44","doi-asserted-by":"crossref","first-page":"6181","DOI":"10.1073\/pnas.95.11.6181","article-title":"The interaction of Arp2\/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments","volume":"95","author":"Mullins","year":"1998","journal-title":"Proc Natl Acad Sci USA"},{"key":"bib45","doi-asserted-by":"publisher","first-page":"E472","DOI":"10.1073\/pnas.1100236108","article-title":"Arp2\/3 complex is bound and activated by two WASP proteins","volume":"108","author":"Padrick","year":"2011","journal-title":"Proc Natl Acad Sci USA"},{"key":"bib46","doi-asserted-by":"publisher","first-page":"426","DOI":"10.1016\/j.molcel.2008.10.012","article-title":"Hierarchical regulation of WASP\/WAVE proteins","volume":"32","author":"Padrick","year":"2008","journal-title":"Mol Cell"},{"key":"bib47","doi-asserted-by":"publisher","first-page":"707","DOI":"10.1146\/annurev.biochem.77.060407.135452","article-title":"Physical mechanisms of signal integration by WASP family proteins","volume":"79","author":"Padrick","year":"2010","journal-title":"Annu Rev Biochem"},{"key":"bib48","doi-asserted-by":"publisher","first-page":"591","DOI":"10.1038\/nsb952","article-title":"A conserved amphipathic helix in WASP\/Scar proteins is essential for activation of Arp2\/3 complex","volume":"10","author":"Panchal","year":"2003","journal-title":"Nat Struct Biol"},{"key":"bib49","doi-asserted-by":"publisher","first-page":"451","DOI":"10.1146\/annurev.biophys.35.040405.101936","article-title":"Regulation of actin filament assembly by Arp2\/3 complex and formins","volume":"36","author":"Pollard","year":"2007","journal-title":"Annu Rev Biophys Biomol Struct"},{"key":"bib50","doi-asserted-by":"publisher","first-page":"453","DOI":"10.1016\/S0092-8674(03)00120-X","article-title":"Cellular motility driven by assembly and disassembly of actin filaments","volume":"112","author":"Pollard","year":"2003","journal-title":"Cell"},{"key":"bib51","doi-asserted-by":"publisher","first-page":"1208","DOI":"10.1126\/science.1175862","article-title":"Actin, a central player in cell shape and movement","volume":"326","author":"Pollard","year":"2009","journal-title":"Science"},{"key":"bib52","doi-asserted-by":"publisher","first-page":"1679","DOI":"10.1126\/science.1066333","article-title":"Crystal structure of Arp2\/3 complex","volume":"294","author":"Robinson","year":"2001","journal-title":"Science"},{"key":"bib53","doi-asserted-by":"publisher","first-page":"26","DOI":"10.1038\/nsmb870","article-title":"Conformational changes in the Arp2\/3 complex leading to actin nucleation","volume":"12","author":"Rodal","year":"2005","journal-title":"Nat Struct Mol Biol"},{"key":"bib54","doi-asserted-by":"publisher","first-page":"221","DOI":"10.1016\/S0092-8674(00)80732-1","article-title":"The interaction between N-WASP and the Arp2\/3 complex links Cdc42-dependent signals to actin assembly","volume":"97","author":"Rohatgi","year":"1999","journal-title":"Cell"},{"key":"bib55","doi-asserted-by":"publisher","first-page":"887","DOI":"10.1083\/jcb.200709092","article-title":"The structural basis of actin filament branching by the Arp2\/3 complex","volume":"180","author":"Rouiller","year":"2008","journal-title":"J Cell Biol"},{"key":"bib56","doi-asserted-by":"publisher","first-page":"6132","DOI":"10.1021\/ac1008749","article-title":"Acidification of the oxygen scavenging system in single-molecule fluorescence studies: in situ sensing with a ratiometric dual-emission probe","volume":"82","author":"Shi","year":"2010","journal-title":"Anal Chem"},{"key":"bib57","doi-asserted-by":"publisher","first-page":"637","DOI":"10.1083\/jcb.200502053","article-title":"Interactions of WASp, myosin-I, and verprolin with Arp2\/3 complex during actin patch assembly in fission yeast","volume":"170","author":"Sirotkin","year":"2005","journal-title":"J Cell Biol"},{"key":"bib58","doi-asserted-by":"crossref","first-page":"638","DOI":"10.1038\/272638a0","article-title":"Polarity of actin at the leading edge of cultured cells","volume":"272","author":"Small","year":"1978","journal-title":"Nature"},{"key":"bib59","doi-asserted-by":"publisher","first-page":"1285","DOI":"10.1073\/pnas.1211164110","article-title":"Pathway of actin filament branch formation by Arp2\/3 complex revealed by single-molecule imaging","volume":"110","author":"Smith","year":"2013","journal-title":"Proc Natl Acad Sci USA"},{"key":"bib60","doi-asserted-by":"crossref","first-page":"4866","DOI":"10.1016\/S0021-9258(18)62016-2","article-title":"The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin","volume":"246","author":"Spudich","year":"1971","journal-title":"J Biol Chem"},{"key":"bib61","doi-asserted-by":"publisher","first-page":"1009","DOI":"10.1083\/jcb.145.5.1009","article-title":"Arp2\/3 complex and actin depolymerizing factor\/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia","volume":"145","author":"Svitkina","year":"1999","journal-title":"J Cell Biol"},{"key":"bib62","doi-asserted-by":"publisher","first-page":"519","DOI":"10.1083\/jcb.148.3.519","article-title":"Actin-dependent propulsion of endosomes and lysosomes by recruitment of N-WASP","volume":"148","author":"Taunton","year":"2000","journal-title":"J Cell Biol"},{"key":"bib63","doi-asserted-by":"publisher","first-page":"E463","DOI":"10.1073\/pnas.1100125108","article-title":"Structural and biochemical characterization of two binding sites for nucleation-promoting factor WASp-VCA on Arp2\/3 complex","volume":"108","author":"Ti","year":"2011","journal-title":"Proc Natl Acad Sci USA"},{"key":"bib64","doi-asserted-by":"publisher","first-page":"2775","DOI":"10.1242\/jcs.107623","article-title":"Actin branching in the initiation and maintenance of lamellipodia","volume":"125","author":"Vinzenz","year":"2012","journal-title":"J Cell Sci"},{"key":"bib65","doi-asserted-by":"publisher","first-page":"87","DOI":"10.1038\/nature07773","article-title":"The rate of N-WASP exchange limits the extent of ARP2\/3-complex-dependent actin-based motility","volume":"458","author":"Weisswange","year":"2009","journal-title":"Nature"},{"key":"bib66","doi-asserted-by":"publisher","first-page":"265","DOI":"10.1038\/385265a0","article-title":"Actin polymerization is induced by Arp2\/3 protein complex at the surface of Listeria monocytogenes","volume":"385","author":"Welch","year":"1997","journal-title":"Nature"},{"key":"bib67","doi-asserted-by":"publisher","first-page":"24168","DOI":"10.1074\/jbc.M502024200","article-title":"Acceleration of yeast actin polymerization by yeast Arp2\/3 complex does not require an Arp2\/3-activating protein","volume":"280","author":"Wen","year":"2005","journal-title":"J Biol Chem"},{"key":"bib68","doi-asserted-by":"publisher","first-page":"236","DOI":"10.1038\/emboj.2011.343","article-title":"Three-dimensional reconstructions of Arp2\/3 complex with bound nucleation promoting factors","volume":"31","author":"Xu","year":"2012","journal-title":"EMBO J"},{"key":"bib69","doi-asserted-by":"crossref","DOI":"10.1016\/j.cell.2013.09.019","article-title":"Structure of a filament-like actin trimer bound to the bacterial effector VopL","author":"Zahm","year":"2013","journal-title":"Cell"},{"key":"bib70","doi-asserted-by":"publisher","first-page":"1903","DOI":"10.1016\/S0960-9822(01)00603-0","article-title":"Different WASP family proteins stimulate different Arp2\/3 complex-dependent actin-nucleating activities","volume":"11","author":"Zalevsky","year":"2001","journal-title":"Curr Biol"}],"container-title":["eLife"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/cdn.elifesciences.org\/articles\/01008\/elife-01008-v1.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/cdn.elifesciences.org\/articles\/01008\/elife-01008-v1.xml","content-type":"application\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/elifesciences.org\/articles\/01008","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,10,11]],"date-time":"2023-10-11T20:41:06Z","timestamp":1697056866000},"score":1,"resource":{"primary":{"URL":"https:\/\/elifesciences.org\/articles\/01008"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,9,3]]},"references-count":70,"alternative-id":["10.7554\/eLife.01008"],"URL":"https:\/\/doi.org\/10.7554\/elife.01008","archive":["CLOCKSS"],"relation":{"has-review":[{"id-type":"doi","id":"10.3410\/f.718112312.793483856","asserted-by":"object"},{"id-type":"doi","id":"10.7554\/eLife.01008.023","asserted-by":"object"},{"id-type":"doi","id":"10.7554\/eLife.01008.022","asserted-by":"object"}]},"ISSN":["2050-084X"],"issn-type":[{"value":"2050-084X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2013,9,3]]},"assertion":[{"value":"2013-05-27","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"2013-07-29","order":1,"name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication History"}},{"value":"2013-09-03","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}],"article-number":"e01008"}}