{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,12]],"date-time":"2026-09-12T04:01:03Z","timestamp":1789185663984,"version":"build-2803163510"},"reference-count":46,"publisher":"Rockefeller University Press","issue":"2","content-domain":{"domain":["rupress.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2004,7,19]]},"abstract":"<jats:p>Shigella, the causative agent of bacillary dysentery, invades epithelial cells in a process involving Src tyrosine kinase signaling. Cortactin, a ubiquitous actin-binding protein present in structures of dynamic actin assembly, is the major protein tyrosine phosphorylated during Shigella invasion. Here, we report that RNA interference silencing of cortactin expression, as does Src inhibition in cells expressing kinase-inactive Src, interferes with actin polymerization required for the formation of cellular extensions engulfing the bacteria. Shigella invasion induced the recruitment of cortactin at plasma membranes in a tyrosine phosphorylation\u2013dependent manner. Overexpression of wild-type forms of cortactin or the adaptor protein Crk favored Shigella uptake, and Arp2\/3 binding\u2013deficient cortactin derivatives or an Src homology 2 domain Crk mutant interfered with bacterial-induced actin foci formation. Crk was shown to directly interact with tyrosine-phosphorylated cortactin and to condition cortactin-dependent actin polymerization required for Shigella uptake. These results point at a major role for a Crk\u2013cortactin complex in actin polymerization downstream of tyrosine kinase signaling.<\/jats:p>","DOI":"10.1083\/jcb.200402073","type":"journal-article","created":{"date-parts":[[2004,7,19]],"date-time":"2004-07-19T18:22:58Z","timestamp":1090261378000},"page":"225-235","update-policy":"https:\/\/doi.org\/10.1083\/jcb.crossmarkpolicy","source":"Crossref","is-referenced-by-count":81,"title":["Cortactin and Crk cooperate to trigger actin polymerization during <i>Shigella<\/i> invasion of epithelial cells"],"prefix":"10.1083","volume":"166","author":[{"given":"Laurence","family":"Bougne\u0300res","sequence":"first","affiliation":[{"name":"1Unite\u0301 de Pathoge\u0301nie Microbienne Mole\u0301culaire, INSERM U389"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ste\u0301phane E.","family":"Girardin","sequence":"additional","affiliation":[{"name":"1Unite\u0301 de Pathoge\u0301nie Microbienne Mole\u0301culaire, INSERM U389"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Scott A.","family":"Weed","sequence":"additional","affiliation":[{"name":"3Department of Craniofacial Biology, University of Colorado Health Sciences Center, Denver, CO 80262"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrei V.","family":"Karginov","sequence":"additional","affiliation":[{"name":"4Department of Microbiology Health Sciences Center, University of Virginia, Charlottesville, VA 22908"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jean-Christophe","family":"Olivo-Marin","sequence":"additional","affiliation":[{"name":"2Unite\u0301 d'Analyse d'Images Quantitative, Institut Pasteur, 75724 Paris Cedex 15, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J. 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