{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,17]],"date-time":"2026-02-17T12:31:14Z","timestamp":1771331474718,"version":"3.50.1"},"reference-count":53,"publisher":"Wiley","issue":"8","license":[{"start":{"date-parts":[[2024,12,18]],"date-time":"2024-12-18T00:00:00Z","timestamp":1734480000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000038","name":"Natural Sciences and Engineering Research Council of Canada","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000038","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Cytoskeleton"],"published-print":{"date-parts":[[2025,8]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:p>Enteropathogenic <jats:styled-content style=\"fixed-case\">\n<jats:italic>Escherichia coli<\/jats:italic>\n<\/jats:styled-content> (EPEC) causes diarrheal disease. Once ingested, these extracellular pathogens attach to the intestinal epithelial cells of their host, collapse the localized microvilli, and generate actin\u2010rich structures within the host cells that are located beneath the attached bacteria, called \u201cpedestals.\u201d Palladin is an actin\u2010associated protein that cross\u2010links and stabilizes actin filaments. This protein also acts as a scaffolding protein for other actin\u2010binding proteins. Here, we examine the role of Palladin during EPEC infections and show that Palladin is co\u2010opted by EPEC. Depletion of Palladin resulted in shorter pedestals, and when Palladin containing mutations in either its actin\u2010 or VASP\u2010binding domains were overexpressed in cells, pedestals decreased in length. Importantly, we show that the overexpression of Palladin in <jats:italic>ArpC2<\/jats:italic>\n<jats:sup>\n<jats:italic>\u2212\/\u2212<\/jats:italic>\n<\/jats:sup> (Arp2\/3 complex\u2013depleted) cells rescued pedestal length. Together, our results demonstrate that Palladin has the ability to rescue pedestal length during EPEC infections when the function of the Arp2\/3 complex is diminished.<\/jats:p>","DOI":"10.1002\/cm.21974","type":"journal-article","created":{"date-parts":[[2024,12,18]],"date-time":"2024-12-18T07:14:04Z","timestamp":1734506044000},"page":"497-512","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Overexpressed Palladin Rescues Enteropathogenic <i>E. coli<\/i> (<scp>EPEC<\/scp>) Pedestal Lengths in <scp>ArpC2<\/scp> Depleted Cells"],"prefix":"10.1002","volume":"82","author":[{"ORCID":"https:\/\/orcid.org\/0009-0009-4547-5898","authenticated-orcid":false,"given":"Kaitlin M.","family":"Bruzzini","sequence":"first","affiliation":[{"name":"Department of Biological Sciences, Centre for Cell Biology, Development, and Disease Simon Fraser University  Burnaby British Columbia Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"S. Tara","family":"Mann","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, Centre for Cell Biology, Development, and Disease Simon Fraser University  Burnaby British Columbia Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Julian A.","family":"Guttman","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, Centre for Cell Biology, Development, and Disease Simon Fraser University  Burnaby British Columbia 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