Identification of INAD Phosphorylation Sites.

<p>A, Representative Coomassie-stained polyacrylamide gel of protein extracts from wild type fly heads that were immunoprecipitated with an α-INAD antibody. The INAD band at ca. 75 kDa was excised, digested with trypsin, and subjected to nanoLC-ESI mass spectrometry. MS/MS spectra of identified phosphopeptides are shown in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0122039#pone.0122039.s002" target="_blank">S2 B Fig</a>., Cartoon of the INAD protein structure showing the positions of PDZ domains (modified from [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0122039#pone.0122039.ref007" target="_blank">7</a>]) and the identified phosphorylation sites. C, INAD amino acid sequence depicting peptides that were identified by mass spectrometry (85.9% sequence coverage, highlighted in yellow) and identified phosphorylation sites indicated by red letters.