Proteomics

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De novo mapping of the apicomplexan Ca2+-responsive proteome: temperature range thermal profiling experiment

ABSTRACT: Apicomplexan parasites cause persistent mortality and morbidity worldwide through diseases including malaria, toxoplasmosis, and cryptosporidiosis. Ca2+ signaling pathways have been repurposed in these eukaryotic pathogens to regulate parasite-specific cellular processes governing the transition between the replicative and lytic phases of the infectious cycle. Despite the presence of conserved Ca2+-responsive proteins, little is known about how specific signaling elements interact to impact pathogenesis. We mapped the Ca2+-responsive proteome of the model apicomplexan T. gondii via time-resolved phosphoproteomics and thermal proteome profiling. The waves of phosphoregulation following PKG activation and stimulated Ca2+ release corroborate known physiological changes but identify specific molecular components in these pathways. Thermal profiling of parasite extracts identified many expected Ca2+-responsive proteins, such as parasite Ca2+-dependent protein kinases. Our approach also identified numerous Ca2+-responsive proteins that are not predicted to bind Ca2+, yet are critical components of the parasite signaling network. We characterized protein phosphatase 1 (PP1) as a Ca2+-responsive enzyme that relocalized to the parasite apex upon Ca2+ store release. Conditional depletion of PP1 revealed that the phosphatase regulates Ca2+ uptake to promote parasite motility. PP1 may thus be partly responsible for Ca2+-regulated serine/threonine phosphatase activity in apicomplexan parasites.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Toxoplasma Gondii Rh

SUBMITTER: Alice Herneisen  

LAB HEAD: Sebastian Lourido

PROVIDER: PXD033713 | Pride | 2022-10-15

REPOSITORIES: Pride

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20190402_10uM_Ca_1_2_15_16_17_18.raw Raw
20190402_10uM_Ca_3_9.raw Raw
20190402_10uM_Ca_4_10.raw Raw
20190402_10uM_Ca_5_11.raw Raw
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Publications

Temporal and thermal profiling of the <i>Toxoplasma</i> proteome implicates parasite Protein Phosphatase 1 in the regulation of Ca<sup>2+</sup>-responsive pathways.

Herneisen Alice L AL   Li Zhu-Hong ZH   Chan Alex W AW   Moreno Silvia N J SNJ   Lourido Sebastian S  

eLife 20220817

Apicomplexan parasites cause persistent mortality and morbidity worldwide through diseases including malaria, toxoplasmosis, and cryptosporidiosis. Ca<sup>2+</sup> signaling pathways have been repurposed in these eukaryotic pathogens to regulate parasite-specific cellular processes governing the replicative and lytic phases of the infectious cycle, as well as the transition between them. Despite the presence of conserved Ca<sup>2+</sup>-responsive proteins, little is known about how specific sig  ...[more]