{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,8]],"date-time":"2026-10-08T01:14:03Z","timestamp":1791422043832,"version":"4.3.3"},"reference-count":33,"publisher":"National Academy of Sciences","issue":"11","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2003,5,27]]},"abstract":"<jats:p>Extension of lamellipodia, an important dissipative process in cell  motility, is driven by the turnover of a polarized dendritic array of actin  filaments. Motility is driven by catalytic cycles of filament attachment to  Wiskott\u2013Aldrich syndrome protein (WASP)-activated actin-related protein  (Arp)2\/3 complex at the leading edge, branch formation, and detachment,  allowing subsequent growth of branched filaments. The morphology, mechanical  strength, and lifetime of the array are determined by the processes of  filament branching, debranching, and treadmilling. All three processes are  controlled by ATP hydrolysis. ATP hydrolysis on F-actin is known to be at the  origin of treadmilling. Here, by using radiolabeled ATP covalently bound to  Arp2\/3, we show that ATP is hydrolyzed on Arp2, not on Arp3, after a delay  following filament branching. Hydrolysis of ATP on Arp2 promotes debranching  of filaments and acts as a clock that controls the stability of dendritic  actin arrays in lamellipodia. Finally, we propose that hydrolysis of ATP on  G-actin in the ternary G-actin\u2013WASP\u2013Arp2\/3 complex on branch  formation destabilizes the WASP\u2013actin interface and energetically  facilitates the detachment step in the branching reaction.<\/jats:p>","DOI":"10.1073\/pnas.1130513100","type":"journal-article","created":{"date-parts":[[2003,5,27]],"date-time":"2003-05-27T13:10:32Z","timestamp":1054041032000},"page":"6337-6342","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":91,"title":["ATP hydrolysis on actin-related protein 2\/3 complex causes debranching of  dendritic actin arrays"],"prefix":"10.1073","volume":"100","author":[{"given":"Christophe","family":"Le Clainche","sequence":"first","affiliation":[{"name":"Dynamique du Cytosquelette et Motilit\u00e9 Cellulaire, Laboratoire d'Enzymologie et Biochimie Structurale, Centre National de la Recherche Scientifique 1, Avenue de la Terrasse, 91198 Gif-sur-Yvette, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dominique","family":"Pantaloni","sequence":"additional","affiliation":[{"name":"Dynamique du Cytosquelette et Motilit\u00e9 Cellulaire, Laboratoire d'Enzymologie et Biochimie Structurale, Centre National de la Recherche Scientifique 1, Avenue de la Terrasse, 91198 Gif-sur-Yvette, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marie-France","family":"Carlier","sequence":"additional","affiliation":[{"name":"Dynamique du Cytosquelette et Motilit\u00e9 Cellulaire, Laboratoire d'Enzymologie et Biochimie Structurale, Centre National de la Recherche Scientifique 1, Avenue de la Terrasse, 91198 Gif-sur-Yvette, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2003,5,12]]},"reference":[{"key":"e_1_3_2_1_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0962-8924(01)02237-1"},{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1038\/35010008"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.biochem.70.1.649"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1059975"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0960-9822(01)00098-7"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.200105148"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1038\/35040061"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.148.3.519"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.200207148"},{"key":"e_1_3_2_10_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.281.5373.105"},{"key":"e_1_3_2_11_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)80732-1"},{"key":"e_1_3_2_12_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.96.7.3739"},{"key":"e_1_3_2_13_2","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.146.6.1319"},{"key":"e_1_3_2_14_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0960-9822(99)80218-8"},{"key":"e_1_3_2_15_2","doi-asserted-by":"publisher","DOI":"10.1038\/35017011"},{"key":"e_1_3_2_16_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi010486b"},{"key":"e_1_3_2_17_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.222652499"},{"key":"e_1_3_2_18_2","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.145.5.1009"},{"key":"e_1_3_2_19_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0006-3495(01)75842-0"},{"key":"e_1_3_2_20_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0960-9822(00)00749-1"},{"key":"e_1_3_2_21_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1066333"},{"key":"e_1_3_2_22_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.C100476200"},{"key":"e_1_3_2_23_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)30017-1"},{"key":"e_1_3_2_24_2","doi-asserted-by":"publisher","DOI":"10.1016\/0006-291X(87)90361-5"},{"key":"e_1_3_2_25_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0960-9822(01)00629-7"},{"key":"e_1_3_2_26_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(01)00605-5"},{"key":"e_1_3_2_27_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0960-9822(01)00022-7"},{"key":"e_1_3_2_28_2","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(93)90544-Z"},{"key":"e_1_3_2_29_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.261419298"},{"key":"e_1_3_2_30_2","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(95)00724-N"},{"key":"e_1_3_2_31_2","unstructured":"Carlsson A. 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