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. 2011 Mar 24;286(19):16914–16928. doi: 10.1074/jbc.M111.218735

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© 2011 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 2. — Phosphorylation of GST-tagged Cx50 C terminus fusion proteins and its mutants in vitro by PKA. A, schematic representation of GST-tagged Cx50 C terminus fusion proteins and its mutants GST-Cx50FS(S395A, GST-Cx50FS(S387A), and GST-Cx50FS(S387A,S395A). cDNA fragments encoding a short C-terminal tail (FS, residues 369–400) of Cx50 were subcloned into GST-tagged expression vector pGEX-2T. Site-directed mutagenesis of serine to alanine was performed by a PCR-based mutagenesis method. B, GST-Cx50FS(S395A), GST-Cx50FS(S387A), and GST-Cx50FS(S387A,S395A) were purified and resolved by SDS-PAGE with Coomassie Blue staining. C, amino acid residues 369–400 of Cx50 in the GST fusion protein and predicted tryptic cleavage sites are indicated (arrows). Both Ser-395 and Ser-387 are located within a PKA consensus site (R(R/K)X(S/T) > RXX(S/T) = RX(S/T)). Their corresponding predicted tryptic peptides are underlined.