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These differing roles are mediated by distinct and discrete binding interactions with aldolase's many binding partners, including actin filaments, Wiskott\u2010Aldrich Syndrome protein (WASP), and Sorting Nexin 9 (SNX9). How these interactions are coordinated on the aldolase homotetramer of 160\u2009kDa is unclear. In this study, the catalytic activity of wild\u2010type aldolase is measured in the presence of actin filaments, and a WASP\u2010derived peptide that binds to aldolase, or both. No appreciable changes in <jats:italic>k<\/jats:italic><jats:sub>cat<\/jats:sub> or <jats:italic>K<\/jats:italic><jats:sub>m<\/jats:sub> values are seen. Then, aldolase variants with substitutions targeting the tryptophan\u2010binding pocket for WASP and SNX9 are created and perturbation of actin filament\u2010, WASP peptide\u2010, and SNX9 peptide\u2010binding are assessed. Those that negatively impacted binding did not show an impact on aldolase catalysis. These results suggest that aldolase can engage in catalysis while simultaneously interacting with cytoskeletal machinery.<\/jats:p>","DOI":"10.1002\/cm.21646","type":"journal-article","created":{"date-parts":[[2020,11,19]],"date-time":"2020-11-19T07:40:59Z","timestamp":1605771659000},"page":"129-141","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Actin filament\u2010 and <scp>Wiskott\u2010Aldrich<\/scp> syndrome <scp>protein\u2010binding<\/scp> sites on fructose\u20101,6\u2010bisphosphate aldolase are functionally distinct from the active site"],"prefix":"10.1002","volume":"78","author":[{"given":"Maggie H.","family":"Hui","sequence":"first","affiliation":[{"name":"Department of Biology Boston University  Boston Massachusetts USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kevin","family":"Rhine","sequence":"additional","affiliation":[{"name":"Program in Cell, Molecular, and Developmental Biology, and Biophysics Johns Hopkins University  Baltimore Maryland USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0598-7241","authenticated-orcid":false,"given":"Dean R.","family":"Tolan","sequence":"additional","affiliation":[{"name":"Department of Biology Boston University  Boston Massachusetts USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2020,12,14]]},"reference":[{"key":"e_1_2_7_2_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1971.tb01522.x"},{"key":"e_1_2_7_3_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1970.tb01016.x"},{"key":"e_1_2_7_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0300-9629(96)00396-9"},{"key":"e_1_2_7_5_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0605301104"},{"key":"e_1_2_7_6_1","doi-asserted-by":"publisher","DOI":"10.1016\/0003-2697(76)90527-3"},{"key":"e_1_2_7_7_1","doi-asserted-by":"publisher","DOI":"10.1091\/mbc.e03-06-0355"},{"key":"e_1_2_7_8_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M506346200"},{"key":"e_1_2_7_9_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi0114877"},{"key":"e_1_2_7_10_1","doi-asserted-by":"publisher","DOI":"10.1016\/0005-2744(74)90270-8"},{"key":"e_1_2_7_11_1","doi-asserted-by":"publisher","DOI":"10.1093\/jxb\/erx015"},{"key":"e_1_2_7_12_1","doi-asserted-by":"publisher","DOI":"10.1002\/prot.21909"},{"key":"e_1_2_7_13_1","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.150.6.1311"},{"key":"e_1_2_7_14_1","doi-asserted-by":"publisher","DOI":"10.1016\/0378-1119(89)90358-2"},{"key":"e_1_2_7_15_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jsb.2017.11.005"},{"key":"e_1_2_7_16_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.cell.2015.12.042"},{"key":"e_1_2_7_17_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi015700a"},{"key":"e_1_2_7_18_1","doi-asserted-by":"publisher","DOI":"10.1093\/oxfordjournals.jbchem.a134260"},{"key":"e_1_2_7_19_1","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(72)80097-8"},{"key":"e_1_2_7_20_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.cellsig.2015.08.019"},{"key":"e_1_2_7_21_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.cmet.2017.10.009"},{"key":"e_1_2_7_22_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M307334200"},{"key":"e_1_2_7_23_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M407430200"},{"key":"e_1_2_7_24_1","doi-asserted-by":"publisher","DOI":"10.1038\/35050590"},{"key":"e_1_2_7_25_1","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/21.9.2277"},{"key":"e_1_2_7_26_1","doi-asserted-by":"publisher","DOI":"10.1152\/ajpcell.00076.2010"},{"key":"e_1_2_7_27_1","doi-asserted-by":"publisher","DOI":"10.1042\/bj20040176"},{"key":"e_1_2_7_28_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)54046-1"},{"key":"e_1_2_7_29_1","doi-asserted-by":"publisher","DOI":"10.1186\/s12936-015-0834-9"},{"issue":"6","key":"e_1_2_7_30_1","first-page":"678","article-title":"Functional in vitro test of calmodulin antagonism: Effect of drugs on interaction between calmodulin and glycolytic enzymes","volume":"33","author":"Orosz F.","year":"1988","journal-title":"Molecular Pharmacology"},{"key":"e_1_2_7_31_1","doi-asserted-by":"publisher","DOI":"10.1016\/B978-0-12-152812-6.50010-X"},{"key":"e_1_2_7_32_1","doi-asserted-by":"publisher","DOI":"10.1023\/B:MCBI.0000009860.86969.72"},{"key":"e_1_2_7_33_1","doi-asserted-by":"publisher","DOI":"10.1007\/PL00000910"},{"key":"e_1_2_7_34_1","doi-asserted-by":"publisher","DOI":"10.1016\/0076-6879(82)85020-9"},{"key":"e_1_2_7_35_1","volume-title":"Interactions among Isozyme\u2010specific residues in Fructose\u20101,6\u2010bisphosphate Aldolase","author":"Pezza J. 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