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The actin-binding protein cortactin interacts with E-cadherin and enables F-actin accumulation at adherens junctions. Here, we were interested to study the broader functional interactions of cortactin in adhesion complexes. In line with literature, we demonstrate that cortactin binds to E-cadherin, and that a posttranslational modification of cortactin, RhoA-induced phosphorylation by protein kinase D1 (PKD1; also known as PRKD1) at S298, impairs adherens junction assembly and supports their dissolution. Two new S298-phosphorylation-dependent interactions were also identified, namely, that phosphorylation of cortactin decreases its interaction with \u03b2-catenin and the actin-binding protein vinculin. In addition, binding of vinculin to \u03b2-catenin, as well as linkage of vinculin to F-actin, are also significantly compromised upon phosphorylation of cortactin. Accordingly, we found that regulation of cell\u2013cell adhesion by phosphorylation of cortactin downstream of RhoA and PKD1 is vitally dependent on vinculin-mediated protein interactions. Thus, cortactin, unexpectedly, is an important integration node for the dynamic regulation of protein complexes during breakdown and formation of adherens junctions.<\/jats:p>","DOI":"10.1242\/jcs.184721","type":"journal-article","created":{"date-parts":[[2016,5,14]],"date-time":"2016-05-14T02:10:13Z","timestamp":1463191813000},"page":"2416-2429","source":"Crossref","is-referenced-by-count":23,"title":["Cortactin is a scaffolding platform for the E-cadherin adhesion complex and is regulated by protein kinase D1 phosphorylation"],"prefix":"10.1242","volume":"129","author":[{"given":"Robert","family":"Sroka","sequence":"first","affiliation":[{"name":"Ulm University 1 Department of Internal Medicine I , , Albert-Einstein-Allee 23, Ulm 89081 , Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Johan","family":"Van Lint","sequence":"additional","affiliation":[{"name":"Katholieke Universiteit Leuven 2 Department of Cellular and Molecular Medicine , , Campus Gasthuisberg O\/N1 - Herestraat 49 bus 901, Leuven 3000 , Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sarah-Fee","family":"Katz","sequence":"additional","affiliation":[{"name":"Ulm University 1 Department of Internal Medicine I , , Albert-Einstein-Allee 23, Ulm 89081 , Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marlon R.","family":"Schneider","sequence":"additional","affiliation":[{"name":"LMU Munich, Gene Center 3 Department for Animal Breeding and Biotechnology , , Feodor-Lynen-Str. 25, Munich 81377 , Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexander","family":"Kleger","sequence":"additional","affiliation":[{"name":"Ulm University 1 Department of Internal Medicine I , , Albert-Einstein-Allee 23, Ulm 89081 , Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stephan","family":"Paschke","sequence":"additional","affiliation":[{"name":"Ulm University 4 Department of Visceral Surgery , , Albert-Einstein-Allee 23, Ulm 89081 , Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas","family":"Seufferlein","sequence":"additional","affiliation":[{"name":"Ulm University 1 Department of Internal Medicine I , , Albert-Einstein-Allee 23, Ulm 89081 , Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7819-4659","authenticated-orcid":false,"given":"Tim","family":"Eiseler","sequence":"additional","affiliation":[{"name":"Ulm University 1 Department of Internal Medicine I , , Albert-Einstein-Allee 23, Ulm 89081 , Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"237","reference":[{"key":"2024061316171633800_JCS184721C1","doi-asserted-by":"publisher","first-page":"1520","DOI":"10.1074\/jbc.271.3.1520","article-title":"Single amino acid substitutions in proteins of the armadillo gene family abolish their binding to alpha-catenin","volume":"271","author":"Aberle","year":"1996","journal-title":"J. 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