Project description:Sponges (Porifera) are early-branching Metazoa who do not posess muscles or neurons, however are able to undergo a whole-body movement that involves the closure of their canal system and collapse of an epithelial tent. In this study we profile proteomic responses of the freshwater sponge Spongilla lacustris during agitation induced movements to elucidate the early evolution of coordination. Results from Thermal Proteome Profiling (TPP) experiments of agitated sponges suggest active secretion during the movement. Here, we use tandem mass tag (TMT) labeling-based quantification of proteins in the medium to systematically measure quantitative differences of secretion before and after agitation induced movement. In total, 146 proteins were detected in the medium, 47 of which were significantly upregulated during the movement.
Project description:Sponges (Porifera) are early-branching Metazoa who do not possess muscles or neurons, however are able to undergo a whole-body movement that involves the closure of their canal system and collapse of an epithelial tent. In this study we profile the proteomic responses of the freshwater sponge Spongilla lacustris during nitric oxide (NO) and agitation induced movements to elucidate the early evolution of coordination in animals. Specifically, we used tandem mass tag (TMT) labeling-based quantification of enriched phosphopeptides to systematically measure quantitative differences in protein phosphorylation. We identified and quantified 12165 unique phosphopeptides in the sponge. NO treatment resulted in quantitative changes of phosphorylation levels on 390 unique phosphopeptides mapping to 270 unique proteins. In turn, agitation led to quantitative changes of phosphorylation levels on 303 unique phosphopeptides (229 proteins).