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. 2010 Dec 1;21(23):4275–4286. doi: 10.1091/mbc.E10-04-0332

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© 2010 by The American Society for Cell Biology

This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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Figure 1. — Expression and activity of ErbB4 isoforms in NR6 cells. (A) Expression of ErbB4 protein in NR6 transfectants was analyzed by Western blotting. (B) Cells were starved overnight without serum and stimulated with or without 50 ng/ml NRG-1 for 10 min. ErbB4 tyrosine phosphorylation was analyzed by immunoprecipitation with an anti-ErbB4 antibody followed by Western blotting with an anti-phosphotyrosine antibody. Membrane was reblotted with an anti-ErbB4 antibody. (C) For in vitro kinase assay, cell lysates were immunoprecipitated with an anti-ErbB4 antibody, incubated with ATP, and analyzed for ErbB4 tyrosine phosphorylation by immunoprecipitation with anti-ErbB4 antibody followed by Western blotting with an anti-phosphotyrosine antibody. (D) Cells were starved overnight and stimulated with or without NRG-1 for indicated time periods. Phosphorylation of Erk, Akt, and p38 was analyzed by Western blotting with phosphospecific antibodies. Subsequently, membranes were reblotted with anti-Erk, anti-Akt, anti-p38, or anti-actin antibodies.