Exploratory phosphoproteomics profiling of Aedes aegypti Malpighian tubules during blood meal processing reveals dramatic transition in function
Fig 5
Changes in TOR signaling, and conservation of rps6 phosphorylation sites.
a. many proteins involved in Tor signaling underwent changes in phosphorylation after blood feeding. The diagram shows important proteins in the Ae. aegypti Tor signaling pathway conserved in other eukaryotic organisms, with the specific residue(s) with changed phosphorylation state PBM. The table contains more information about each phosphorylated protein, including the Uniprot ID, and the change in phosphorylation of each residue at 1hr PBM relative to unfed, and at 24hr PBM relative to unfed. Green arrowheads represent at least 1.5-fold increased number of phosphorylated residues detected relative to the same position in unfed samples, and red arrowheads represent at least 1.5-fold decreased number of phosphorylated residues detected relative to the same position in unfed samples. b. Neighbor joining tree generated by the COBALT multiple sequence alignment tool (Papadopoulos & Agarwala, 2007), which illustrates the conservation of S6 in several orders of eukaryotes. c. Multiple sequence alignment of a portion of the S6 protein which is enriched in phosphorylation sites. This region contains four serine residues that are phosphorylated in mammalian S6 (marked by “P” above the alignment). All four of these residues are conserved in Ae. aegypti, and three of them (S231, S235, and S237) underwent changes in phosphorylation in MTs after blood feeding.