{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,19]],"date-time":"2026-09-19T03:23:06Z","timestamp":1789788186590,"version":"4.0.1"},"reference-count":50,"publisher":"Wiley","issue":"8","license":[{"start":{"date-parts":[[2013,6,12]],"date-time":"2013-06-12T00:00:00Z","timestamp":1370995200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J of Cellular Biochemistry"],"published-print":{"date-parts":[[2013,8]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>In addition to its roles in sugar metabolism, fructose\u20101,6\u2010bisphosphate aldolase (aldolase) has been implicated in cellular functions independent from these roles, termed \u201cmoonlighting functions.\u201d These moonlighting functions likely involve the known aldolase\u2013actin interaction, as many proteins with which aldolase interacts are involved in actin\u2010dependent processes. Specifically, aldolase interacts both in vitro and in cells with Wiskott\u2013Aldrich Syndrome Protein (WASP), a protein involved in controlling actin dynamics, yet the function of this interaction remains unknown. Here, the effect of aldolase on WASP\u2010dependent processes in vitro and in cells is investigated. Aldolase inhibits WASP\/Arp2\/3\u2010dependent actin polymerization in vitro. In cells, knockdown of aldolase results in a decreased rate of cell motility and cell spreading, two WASP\u2010dependent processes. Expression of exogenous aldolase rescues these defects. Whether these effects of aldolase on WASP\u2010dependent processes were due to aldolase catalysis or moonlighting functions is tested using aldolase variants defective in either catalytic or actin\u2010binding activity. While the actin\u2010binding deficient aldolase variant is unable to inhibit actin polymerization in vitro and is unable to rescue cell motility defects in cells, the catalytically inactive aldolase is able to perform these functions, providing evidence that aldolase moonlighting plays a role in WASP\u2010mediated processes. J. Cell. Biochem. 114: 1928\u20131939, 2013. \u00a9 2013 Wiley Periodicals, Inc.<\/jats:p>","DOI":"10.1002\/jcb.24538","type":"journal-article","created":{"date-parts":[[2013,3,14]],"date-time":"2013-03-14T09:36:27Z","timestamp":1363253787000},"page":"1928-1939","source":"Crossref","is-referenced-by-count":37,"title":["Aldolase sequesters WASP and affects WASP\/Arp2\/3\u2010stimulated actin dynamics"],"prefix":"10.1002","volume":"114","author":[{"given":"Carolyn Ritterson","family":"Lew","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dean R.","family":"Tolan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2013,6,12]]},"reference":[{"key":"e_1_2_6_2_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.270.35.20459"},{"key":"e_1_2_6_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/1046-5928(92)90009-L"},{"key":"e_1_2_6_4_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M700195200"},{"key":"e_1_2_6_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/0003-2697(76)90527-3"},{"key":"e_1_2_6_6_1","doi-asserted-by":"publisher","DOI":"10.1042\/bj1560527"},{"key":"e_1_2_6_7_1","doi-asserted-by":"publisher","DOI":"10.1091\/mbc.E03-06-0355"},{"key":"e_1_2_6_8_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M506346200"},{"key":"e_1_2_6_9_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.cell.2008.06.054"},{"key":"e_1_2_6_10_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0378-1119(97)00184-4"},{"key":"e_1_2_6_11_1","first-page":"1464","volume-title":"Methods of enzymatic analysis","author":"Gutman I","year":"1983"},{"key":"e_1_2_6_12_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi991843"},{"key":"e_1_2_6_13_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.biochem.70.1.649"},{"key":"e_1_2_6_14_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.abb.2004.11.022"},{"key":"e_1_2_6_15_1","doi-asserted-by":"publisher","DOI":"10.1016\/S1097-2765(03)00113-8"},{"key":"e_1_2_6_16_1","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.151.2.249"},{"key":"e_1_2_6_17_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.274.25.17742"},{"key":"e_1_2_6_18_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi015700a"},{"key":"e_1_2_6_19_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0008-6363(96)00137-X"},{"key":"e_1_2_6_20_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1986.tb10462.x"},{"key":"e_1_2_6_21_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M702598200"},{"key":"e_1_2_6_22_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M008768200"},{"key":"e_1_2_6_23_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M303871200"},{"key":"e_1_2_6_24_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M307334200"},{"key":"e_1_2_6_25_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M407430200"},{"key":"e_1_2_6_26_1","doi-asserted-by":"publisher","DOI":"10.1038\/35074551"},{"key":"e_1_2_6_27_1","doi-asserted-by":"publisher","DOI":"10.1152\/ajpcell.00076.2010"},{"key":"e_1_2_6_28_1","doi-asserted-by":"publisher","DOI":"10.1042\/bj20040176"},{"key":"e_1_2_6_29_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbrc.2007.10.086"},{"key":"e_1_2_6_30_1","unstructured":"MorrisAJ.1995. 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