Figure 5 : A burst of tyrosine phosphorylation in Trichoplax.

From: Deep proteome profiling of Trichoplax adhaerens reveals remarkable features at the origin of metazoan multicellularity

Figure 5

(a) Replicate measurements of tyrosine phosphorylation by SCX; in the first bar is the combined result of three independent SCX experiments (n=2177), in the second bar is the first trypsin experiment (n=1331), in the third bar is the Lys-N experiment (n=881) and in the fourth bar is an additional trypsin repeat experiment (n=123); n=total number of unique phosphosites (S, T, Y). (b) Compared with other organisms Trichoplax exhibits a high percentage (3.9%) of tyrosine amino acids in its genome (red bars). The percentage of detected tyrosine phosphosites in Trichoplax phosphoproteomics data sets is four- to fivefold higher than detected in large-scale phosphoproteomics data sets for other organisms, including H. sapiens14,35, M. musculus13, D. melanogaster11 and S. cerevisiae36 (blue bars, Supplementary Data 4). Only species for which comprehensive protein phosphorylation data is also available, obtained using alike protocols, are shown37,38,39,40,41. (c) Trichoplax contains a relative high number of readers (SH2 phosphotyrosine recognition domains) and erasers (tyrosine phosphatases), compared with writers (tyrosine kinases) involved in tyrosine signalling. Tyrosine-kinase domains, SH2 domains and protein tyrosine phosphatase domains were detected using HMM models from SMART28 using the online SMART tool (http://smart.embl-heidelberg.de/). Inset shows phosphotyrosine signalling as a tripartite system comprising tyrosine kinase (writer), tyrosine phosphatase (eraser) and SH2 domain (reader).