Fig. 1: Identification and characterization of the domain structures of the AMPK complex in T. gondii. | Nature Communications

Fig. 1: Identification and characterization of the domain structures of the AMPK complex in T. gondii.

From: Rapid metabolic reprogramming mediated by the AMP-activated protein kinase during the lytic cycle of Toxoplasma gondii

Fig. 1

a–c domain structures of the three subunits of Toxoplama AMPK compared with their corresponding orthologs in other eukaryotes. The human (Homo sapiens, Hs), yeast (Saccharomyces cerevisiae, Sc) and Plasmodium (Pasmodium berghei, Pb) proteins are included for comparison. A sequence alignment (done by Clustal X2) of the activation loop in the kinase domain of AMPKα, along with the conserved threonine residue that is subjected to phosphorylation regulation is provided in a. d transgenic strains expressing TgAMPKα-Ty, TgAMPKβ-Ty or TgAMPKγ-HA were individually used in co-IP (using antibodies against the corresponding epitope tags) experiments to identify proteins interacting with each of the Toxoplasma AMPK subunits. Selected hits from these co-IP experiments identified by mass spectrometry (MS) were shown and the numbers denote the number of unique peptides derived from MS analyses that matched the corresponding hits. All these hits were not identified in the control experiments involving untagged parental strains and a full list of the hits are provided in Supplementary data 1. e recognition of TgAMPKα by the phospho-AMPKα(Thr172) monoclonal antibody that recognizes phosphorylated HsAMPKα, as determined by Western blotting on purified extracellular parasites (Toxoplasma) and host cells. Source data are provided as a Source data file.

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