{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,26]],"date-time":"2026-02-26T20:17:47Z","timestamp":1772137067850,"version":"3.50.1"},"reference-count":54,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2012,1,3]],"date-time":"2012-01-03T00:00:00Z","timestamp":1325548800000},"content-version":"vor","delay-in-days":732,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biology of the Cell"],"published-print":{"date-parts":[[2010,1]]},"abstract":"<jats:p>\n                    <jats:italic>Background information<\/jats:italic>\n                    . The appropriate regulation of cell\u2013cell adhesion is an important event in the homoeostasis of different cell types. In epithelial cells, tight adhesion mediated by E\u2010cadherin receptors is essential for the differentiation and functionality of epithelial sheets. Upon assembly of cadherin\u2010mediated cell\u2013cell contacts, it is well established that the small GTPases Rho and Rac are activated and are necessary for junction stability. However, the role of the small GTPase Cdc42 in cadherin adhesion is less clear. Cdc42 can be activated by E\u2010cadherin in a breast tumour cell line, but the requirement for Cdc42 function for new junction assembly or maintenance has been contradictory. Cdc42 participation in cell\u2013cell contacts has been inferred from the presence of filopodia, the typical F\u2010actin structure induced by Cdc42 activation, as cells approach each other to establish cell\u2013cell contacts. Yet, under these conditions, the contribution of migration to filopodia protrusion cannot be excluded and the results are difficult to interpret.\n                  <\/jats:p>\n                  <jats:p>\n                    <jats:italic>Results<\/jats:italic>\n                    . In the present study, we set out to address (a) whether Cdc42 is activated by new E\u2010cadherin cell\u2013cell contacts when junction assembly occurs without prior migration and (b) whether Cdc42 function is necessary for cadherin stability. We found that junction formation in confluent keratinocytes or upon E\u2010cadherin clustering decreased Cdc42\u2010GTP levels. In the absence of serum\u2010 and migration\u2010induced Cdc42 activation, we demonstrated that cell\u2013cell contacts do not induce filopodia or require Cdc42 function to assemble.\n                  <\/jats:p>\n                  <jats:p>\n                    <jats:italic>Conclusion<\/jats:italic>\n                    . We conclude that Cdc42 does not participate in the early events that initiate stable cadherin adhesion in keratinocytes. Yet, it is feasible that Cdc42 may be activated at later time points or by other receptors. Cdc42 can then participate in additional functions during polarization, such as Golgi re\u2010positioning or basolateral trafficking.\n                  <\/jats:p>","DOI":"10.1042\/bc20090048","type":"journal-article","created":{"date-parts":[[2009,7,9]],"date-time":"2009-07-09T05:08:14Z","timestamp":1247116094000},"page":"13-24","source":"Crossref","is-referenced-by-count":10,"title":["Newly formed E\u2010cadherin contacts do not activate Cdc42 or induce filopodia protrusion in human keratinocytes\n                    <sup>1<\/sup>"],"prefix":"10.1111","volume":"102","author":[{"given":"Jennifer","family":"Erasmus","sequence":"first","affiliation":[]},{"given":"Sandra","family":"Aresta","sequence":"additional","affiliation":[]},{"given":"Sebastien","family":"Nola","sequence":"additional","affiliation":[]},{"given":"Emmanuelle","family":"Caron","sequence":"additional","affiliation":[]},{"given":"Vania M. 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