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. 2012 Aug 17;82(3):428–437. doi: 10.1124/mol.112.077966

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Fig. 1. — A, sequence alignment of predicted PKC site on wild-type Kv11.1, Kv11.1-R887H, and consensus sequence for phosphorylation by PKC recognized by the pS(PKC) antibody. X indicates any amino acid, and hyd indicates an amino acid with a hydrophobic side chain. B, electrospray ionization-MS/MS spectrum of the ion m/z 365.7. The m/z 365.7 precursor ion corresponds in mass to the doubly protonated peptide containing residues 887 to 891 with the addition of a single phosphorylation (mass 729.4). The base peak in the spectrum at m/z 316.7 corresponds to the neutral loss of H₃PO₄ from the precursor. The extensive y-series fragment ions, with and without loss of H₃PO₄, localize the site of phosphorylation to Ser890. C, analysis of Kv11.1 or Kv11.1-HA-S890A channel phosphorylation in CHO cells. D, analysis of Kv11.1 phosphorylation in CHO cells expressing shRNA targeting PKCα. Blots shown are representative of three experiments. E, densitometry analysis of phosphorylated Kv11.1-HA-WT, Kv11.1-HA-S890A, or Kv11.1-HA-WT in cells expressing shRNA (shRNAPKAα) targeting PKCα relative to total protein F, densitometry analysis of PKCα protein in cells expressing shRNA PKAα compared with control cells. contr., control; IP, immunoprecipitation; IB, immunoblot.