Fig. 7: TgAMPKγ depletion affects the phosphorylation of multiple proteins in Toxoplasma.
Alteration of the phosphorylation of selected sugar catabolism proteins (a) and biomass synthesis proteins (b) at indicated positions after TgAMPKγ degradation, as determined by phosphoproteomics on needle released AMPKγ-mAID parasites pretreated with or without IAA for 48 h. Extracted parasite proteins from n = 3 sets of independent samples (each set contained one sample for IAA treated parasites and one for nontreated parasites) were trypsin digested and labeled with six plex tandem mass tags (TMT). Then, phospho-peptides were enriched by TiO2 and IMAC, and quantified by LC-MS/MS. The abundance change (expressed as log2 fold change) and the corresponding p-value (determined by Empirical Bayes two-tailed tests in the limma package) (expressed as -Lg p-value) of each phospho-peptide after TgAMPKγ depletion (+IAA/-IAA) were plotted. Each condition was tested n = 3 times independently. GT1 glucose transporter 1, ACS Acetyl-coenzyme A synthetase, ALD fructose-1,6-bisphosphate aldolase, PYK1 pyruvate kinase 1, PDK pyruvate dehydrogenase kinase, 6PGD 6-phosphogluconate dehydrogenase, eIF eukaryotic initiation factor, CEPT choline/ethanolamine phosphotransferase, FAAL Fatty acyl-AMP ligase.
