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Isothermal titration calorimetry showed that the CA motif from the C\u00a0terminus of fission yeast WASP (Wsp1p) bound to fission yeast and bovine Arp2\/3 complex with a stoichiometry of 2 to 1 and very different affinities for the two sites (\n                    <jats:italic>K<\/jats:italic>\n                    <jats:sub>d<\/jats:sub>\n                    s of 0.13 and 1.6\u00a0\u03bcM for fission yeast Arp2\/3 complex). Equilibrium binding, kinetic, and cross-linking experiments showed that (\n                    <jats:italic>i<\/jats:italic>\n                    ) CA at high-affinity site 1 inhibited Arp2\/3 complex binding to actin filaments, (\n                    <jats:italic>ii<\/jats:italic>\n                    ) low-affinity site 2 had a higher affinity for CA when Arp2\/3 complex was bound to actin filaments, and (\n                    <jats:italic>iii<\/jats:italic>\n                    ) Arp2\/3 complex had a much higher affinity for free CA than VCA cross-linked to an actin monomer. Crystal structures showed the C\u00a0terminus of CA bound to the low-affinity site 2 on Arp3 of bovine Arp2\/3 complex. The C helix is likely to bind to the barbed end groove of Arp3 in a position for VCA to deliver the first actin subunit to the daughter filament.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1100125108","type":"journal-article","created":{"date-parts":[[2011,6,15]],"date-time":"2011-06-15T23:05:03Z","timestamp":1308179103000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":137,"title":["Structural and biochemical characterization of two binding sites for nucleation-promoting factor WASp-VCA on Arp2\/3 complex"],"prefix":"10.1073","volume":"108","author":[{"given":"Shih-Chieh","family":"Ti","sequence":"first","affiliation":[{"name":"Departments of Molecular, Cellular, and Developmental Biology, Cell Biology, and Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8103"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christopher T.","family":"Jurgenson","sequence":"additional","affiliation":[{"name":"Departments of Molecular, Cellular, and Developmental Biology, Cell Biology, and Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8103"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bradley J.","family":"Nolen","sequence":"additional","affiliation":[{"name":"Departments of Molecular, Cellular, and Developmental Biology, Cell Biology, and Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8103"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas D.","family":"Pollard","sequence":"additional","affiliation":[{"name":"Departments of Molecular, Cellular, and Developmental Biology, Cell Biology, and Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8103"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2011,6,15]]},"reference":[{"key":"e_1_1_2_17_12_1_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.biophys.35.040405.101936"},{"key":"e_1_1_2_17_12_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.molcel.2008.10.012"},{"key":"e_1_1_2_17_12_3_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1066333"},{"key":"e_1_1_2_17_12_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.str.2008.02.013"},{"key":"e_1_1_2_17_12_5_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.1100236108"},{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"1347","DOI":"10.1016\/S0960-9822(98)00015-3","article-title":"Scar1 and the related Wiskott\u2013Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2\/3 complex","volume":"8","author":"Machesky L","year":"1998","unstructured":"L Machesky, R Insall, Scar1 and the related Wiskott\u2013Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2\/3 complex. 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