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. 2009 Apr 20;185(2):357–370. doi: 10.1083/jcb.200809110

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© 2009 Chan et al.

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

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Figure 7. — FAK regulates a switch in tyrosine phosphorylation at focal adhesions and invadopodia. (A) Cell lysates from MTLn3 cells transiently transfected with control siRNA (Ctlsi) or FAK siRNA (FAKsi) were analyzed by immunoblotting (IB) or immunoprecipitation (IP)/immunoblotting and probed with phospho-specific antibodies anti-pY397 FAK, anti-pY416 Src, anti-pY410 p130Cas, anti-pY31 paxillin, anti-pY421 cortactin, or antiphosphotyrosine and antibodies to total proteins anti-FAK, anti-Src, anti-p130Cas, antipaxillin, anticortactin, or anti-Tks5/FISH. (B) Quantification of immunoblots or immunoprecipitation/immunoblots is expressed as fold change in phosphorylation to total protein. Fold change was determined by the ratio of normalized phosphorylation to total protein in FAK siRNA compared with control siRNA. Data shown are means ± SEM of three independent experiments.