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. 2014 Sep 25;16:443. doi: 10.1186/s13058-014-0443-5

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© Tornillo et al.; licensee BioMed Central Ltd. 2014

This article is published under license to BioMed Central Ltd. The licensee has exclusive rights to distribute this article, in any medium, for 6 months following its publication. After this time, the article is available under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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p130Cas/BCAR1 and Nedd9 structural features and main interacting proteins. Schematic representation of Cas protein main domains: an amino-terminal SH3 domain followed by a proline-rich region (PRR), a substrate domain (SD), a serine rich region (SRR), and a carboxy-terminal domain (CT). The main proteins whose interaction has been demonstrated for both p130Cas and Nedd9 are indicated in black, the interactors specific for p130Cas are in red and those specific for Nedd9 are in green. Noteworthy, p125FAK binds to the SH3 domain while the Src family kinases bind to the CT domain. The substrate domain with the multiple YxxP motifs represents the site where Src family kinases extensively phosphorylate Cas proteins.