{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T06:13:28Z","timestamp":1790748808230,"version":"4.1.0"},"reference-count":46,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2016,1,11]],"date-time":"2016-01-11T00:00:00Z","timestamp":1452470400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100000261","name":"Multiple Sclerosis Society of Canada","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000261","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000024","name":"Canadian Institutes of Health Research","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000024","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Neurochemistry"],"published-print":{"date-parts":[[2016,2]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:sec><jats:label\/><jats:p>Integrin\u2010linked kinase (<jats:styled-content style=\"fixed-case\">ILK<\/jats:styled-content>), a focal adhesion protein, brokers the link between cytoskeleton, cell membrane, and extracellular environment. Here, we demonstrate a role for <jats:styled-content style=\"fixed-case\">ILK<\/jats:styled-content> in laminin\u20102\u2010mediated adhesion in primary murine oligodendrocytes (<jats:styled-content style=\"fixed-case\">OL<\/jats:styled-content>s) \u2013 with <jats:styled-content style=\"fixed-case\">ILK<\/jats:styled-content> loss leading to severe defects in process branching and outgrowth. These defects were partially recovered when the <jats:styled-content style=\"fixed-case\">ILK<\/jats:styled-content>\u2010depleted <jats:styled-content style=\"fixed-case\">OL<\/jats:styled-content>s were instead grown on the non\u2010integrin\u2010activating substrate poly\u2010<jats:sc>l<\/jats:sc>\u2010lysine. Intriguingly, <jats:styled-content style=\"fixed-case\">ILK<\/jats:styled-content> loss on the neutral poly\u2010<jats:sc>l<\/jats:sc>\u2010lysine substrate led to swelling at the tips of <jats:styled-content style=\"fixed-case\">OL<\/jats:styled-content> processes, which we identified as enlarged growth cones. Employing the bloated <jats:styled-content style=\"fixed-case\">ILK<\/jats:styled-content>\u2010depleted growth cones as template, we demonstrate the appearance of distinct cytoskeletal domains within <jats:styled-content style=\"fixed-case\">OL<\/jats:styled-content> growth cones bearing classic neuronal growth cone architecture. Further, microtubule organization was severely perturbed following <jats:styled-content style=\"fixed-case\">ILK<\/jats:styled-content> loss, with centripetal microtubule looping and failure to bundle occurring in a laminin\u20102\u2010independent manner. Together, our work highlights differences in specific aspects of <jats:styled-content style=\"fixed-case\">OL<\/jats:styled-content> biology as driven by laminin\u20102\u2010dependent or independent <jats:styled-content style=\"fixed-case\">ILK<\/jats:styled-content> governed mechanisms. We also reinforce the idea of <jats:styled-content style=\"fixed-case\">OL<\/jats:styled-content>s as growth cone bearing cells and describe the neuronal\u2010like cytoskeleton therein. Finally, we demonstrate a role for <jats:styled-content style=\"fixed-case\">ILK<\/jats:styled-content> in <jats:styled-content style=\"fixed-case\">OL<\/jats:styled-content> growth cone maturation through microtubule regulation, the loss of which translates to decreased process length and myelin production capacity.<\/jats:p><\/jats:sec><jats:sec><jats:label\/><jats:p>\n<jats:boxed-text content-type=\"graphic\" position=\"anchor\"><jats:graphic xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" mimetype=\"image\/png\" position=\"anchor\" specific-use=\"enlarged-web-image\" xlink:href=\"graphic\/jnc13446-fig-0009-m.png\"><jats:alt-text>image<\/jats:alt-text><\/jats:graphic><\/jats:boxed-text>\nWe describe herein how different substrates fundamentally alter the oligodendrocyte's response to loss of integrin\u2010linked kinase (ILK). On laminin\u20102 (Ln\u20102), ILK\u2010depleted oligodendrocytes appear stunted and malformed, while on the non\u2010integrin\u2010activating substrate PLL branching and membrane formation are restored. We also reinforce the idea of oligodendrocytes as growth cone\u2010bearing cells, detailing the growth cone's cytoskeletal architecture. Strikingly, loss of ILK on poly\u2010<jats:sc>l<\/jats:sc>\u2010lysine leads to growth cone swelling, the structure's size and motility rendered less dynamic. Together, our work helps reconcile the phenotypic discrepancy between ILK loss <jats:italic>in\u00a0vitro<\/jats:italic> and <jats:italic>in\u00a0vivo<\/jats:italic>, informs on the oligodendrocyte's growth cone, and ascribes a role for ILK in growth cone dynamics.<\/jats:p><jats:p><jats:bold>Cover Image<\/jats:bold> for this issue: doi: <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"doi\" xlink:href=\"10.1111\/jnc.13304\">10.1111\/jnc.13304<\/jats:ext-link>.<\/jats:p><\/jats:sec>","DOI":"10.1111\/jnc.13446","type":"journal-article","created":{"date-parts":[[2015,11,28]],"date-time":"2015-11-28T07:28:42Z","timestamp":1448695722000},"page":"536-549","source":"Crossref","is-referenced-by-count":18,"title":["Integrin\u2010linked kinase regulates oligodendrocyte cytoskeleton, growth cone, and adhesion dynamics"],"prefix":"10.1111","volume":"136","author":[{"given":"John\u2010Paul","family":"Michalski","sequence":"first","affiliation":[{"name":"Ottawa Hospital Research Institute Ottawa Ontario Canada"},{"name":"Department of Cellular and Molecular Medicine University of Ottawa Ottawa Ontario Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sarah E.","family":"Cummings","sequence":"additional","affiliation":[{"name":"Ottawa Hospital Research Institute Ottawa Ontario Canada"},{"name":"Department of Cellular and Molecular Medicine University of Ottawa Ottawa Ontario Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ryan W.","family":"O'Meara","sequence":"additional","affiliation":[{"name":"Ottawa Hospital Research Institute Ottawa Ontario Canada"},{"name":"Department of Cellular and Molecular Medicine University of Ottawa Ottawa Ontario Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rashmi","family":"Kothary","sequence":"additional","affiliation":[{"name":"Ottawa Hospital Research Institute Ottawa Ontario Canada"},{"name":"Department of Cellular and Molecular Medicine University of Ottawa Ottawa Ontario Canada"},{"name":"Department of Medicine University of Ottawa Ottawa Ontario Canada"},{"name":"University of Ottawa Centre for Neuromuscular Disease Ottawa Ontario Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2016,1,11]]},"reference":[{"key":"e_1_2_7_2_1","doi-asserted-by":"publisher","DOI":"10.1038\/ncb2646"},{"key":"e_1_2_7_3_1","doi-asserted-by":"publisher","DOI":"10.1002\/glia.20885"},{"key":"e_1_2_7_4_1","doi-asserted-by":"publisher","DOI":"10.1002\/jnr.1217"},{"key":"e_1_2_7_5_1","doi-asserted-by":"publisher","DOI":"10.1002\/jnr.20080"},{"key":"e_1_2_7_6_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.tcb.2006.03.002"},{"key":"e_1_2_7_7_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.devcel.2008.05.016"},{"key":"e_1_2_7_8_1","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.200807010"},{"key":"e_1_2_7_9_1","doi-asserted-by":"publisher","DOI":"10.1242\/dev.02819"},{"key":"e_1_2_7_10_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.devcel.2013.05.013"},{"key":"e_1_2_7_11_1","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.200304021"},{"key":"e_1_2_7_12_1","doi-asserted-by":"publisher","DOI":"10.1002\/jnr.490240211"},{"key":"e_1_2_7_13_1","doi-asserted-by":"publisher","DOI":"10.1002\/jnr.490240212"},{"key":"e_1_2_7_14_1","doi-asserted-by":"publisher","DOI":"10.1002\/jnr.22022"},{"key":"e_1_2_7_15_1","doi-asserted-by":"publisher","DOI":"10.1002\/glia.20293"},{"key":"e_1_2_7_16_1","doi-asserted-by":"publisher","DOI":"10.1042\/BST20130062"},{"key":"e_1_2_7_17_1","doi-asserted-by":"publisher","DOI":"10.1242\/jcs.112.19.3373"},{"key":"e_1_2_7_18_1","doi-asserted-by":"publisher","DOI":"10.1002\/glia.20824"},{"key":"e_1_2_7_19_1","doi-asserted-by":"publisher","DOI":"10.1177\/1073858403260751"},{"key":"e_1_2_7_20_1","doi-asserted-by":"crossref","first-page":"2417","DOI":"10.1242\/jcs.110.19.2417","article-title":"Dissociation of LPA\u2010induced cytoskeletal contraction from stress fiber formation by differential localization of RhoA","volume":"110","author":"Kranenburg O.","year":"1997","journal-title":"J. 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