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. 2016 Sep 13;14(1):21. doi: 10.1186/s12964-016-0144-z

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© The Author(s). 2016

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. 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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Fig. 2 — Translocation of CalDAG-GEFI and Rap1GAP2 is independent of VASP. Platelets from wild-type (WT) or VASP-deficient mice (VASP KO) stimulated or not with thrombin (0.01 U/ml, 30s) were broken by sonication in detergent-free buffer. Lysates were spun at 100,000 g for 1 h. Cytosolic (supernatant) and crude membrane fractions (pellet) were collected and re-suspended in Laemmli buffer. Proteins were separated by 12 % SDS-PAGE, transferred to PVDF membranes, which were subjected to immunoblotting with one of the following Abs: anti-Rap1GAP2, anti-Rap1b or anti-CalDAG-GEFI. The Western blots show the results of one representative experiment (out of three). Protein loading controls (Ponceau S red staining of the blots) are shown in the bottom panels