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Quantitative Phosphoproteomics of whole-body sponge collapse

ABSTRACT: 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).

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Spongilla Lacustris

TISSUE(S): Whole Body

SUBMITTER: Frank Stein

LAB HEAD: Detlev Arendt

PROVIDER: PXD044171 | Pride | 2024-01-04

REPOSITORIES: Pride

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			Action	DRS
	Lara_211122_S2984_CP_Sponge_contraction_F1.raw	Raw
	Lara_211122_S2984_CP_Sponge_contraction_F2.raw	Raw
	Lara_211122_S2984_CP_Sponge_contraction_F3.raw	Raw
	Lara_211122_S2984_CP_Sponge_contraction_F4.raw	Raw
	Lara_211122_S2984_CP_Sponge_contraction_F5.raw	Raw

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