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. 2010 Aug 24;285(46):35374–35385. doi: 10.1074/jbc.M110.148445

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© 2010 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 3. — SPRED1 and -2 interact endogenously and directly with DYRK1A. A, PC-3 cell lysates were immunoprecipitated with anti-SPRED1 and -2 antibodies, and the immunoprecipitated (IP) proteins and the WCL were subjected to SDS-PAGE and immunoblotted (IB) with anti-DYRK1A antibody. B, PC-3 cell lysates were immunoprecipitated with anti-DYRK1A antibody. The immunoprecipitates and the WCL were separated on SDS-PAGE and analyzed by immunoblotting with anti-SPRED1 and -SPRED2, respectively. Closed triangle indicates DYRK1A band; open triangle indicates SPRED1; block arrow indicates SPRED2. The HA-tagged DYRK1A and FLAG-tagged SPRED1 and -2 in the WCL are used as positive controls to indicate that the correct protein bands are present in the immunocomplex. C and D, direct association of DYRK1A and SPRED1 and -2 in vitro. Binding of in vitro translated HA-tagged DYRK1A to FLAG-tagged SPRED1 (C) and SPRED2 (D) proteins in the transcription and translation (TnT) assay. TnT reaction products and anti-FLAG immunoprecipitates were subjected to SDS-PAGE and immunoblotted with anti-HA and anti-FLAG.