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Ca\n                    <jats:sup>2+<\/jats:sup>\n                    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\n                    <jats:sup>2+<\/jats:sup>\n                    -responsive proteins, little is known about how specific signaling elements interact to impact pathogenesis. We mapped the Ca\n                    <jats:sup>2+<\/jats:sup>\n                    -responsive proteome of the model apicomplexan\n                    <jats:italic>Taxoplasma gondii<\/jats:italic>\n                    via time-resolved phosphoproteomics and thermal proteome profiling. The waves of phosphoregulation following PKG activation and stimulated Ca\n                    <jats:sup>2+<\/jats:sup>\n                    release corroborate known physiological changes but identify specific proteins operating in these pathways. Thermal profiling of parasite extracts identified many expected Ca\n                    <jats:sup>2+<\/jats:sup>\n                    -responsive proteins, such as parasite Ca\n                    <jats:sup>2+<\/jats:sup>\n                    -dependent protein kinases. Our approach also identified numerous Ca\n                    <jats:sup>2+<\/jats:sup>\n                    -responsive proteins that are not predicted to bind Ca\n                    <jats:sup>2+<\/jats:sup>\n                    , yet are critical components of the parasite signaling network. We characterized protein phosphatase 1 (PP1) as a Ca\n                    <jats:sup>2+<\/jats:sup>\n                    -responsive enzyme that relocalized to the parasite apex upon Ca\n                    <jats:sup>2+<\/jats:sup>\n                    store release. Conditional depletion of PP1 revealed that the phosphatase regulates Ca\n                    <jats:sup>2+<\/jats:sup>\n                    uptake to promote parasite motility. PP1 may thus be partly responsible for Ca\n                    <jats:sup>2+<\/jats:sup>\n                    -regulated serine\/threonine phosphatase activity in apicomplexan parasites.\n                  <\/jats:p>","DOI":"10.7554\/elife.80336","type":"journal-article","created":{"date-parts":[[2022,8,17]],"date-time":"2022-08-17T08:15:12Z","timestamp":1660724112000},"update-policy":"https:\/\/doi.org\/10.7554\/elife.80336","source":"Crossref","is-referenced-by-count":34,"title":["Temporal and thermal profiling of the Toxoplasma proteome implicates parasite Protein Phosphatase 1 in the regulation of Ca2+-responsive pathways"],"prefix":"10.7554","volume":"11","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-3368-0893","authenticated-orcid":true,"given":"Alice L","family":"Herneisen","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/04vqm6w82","id-type":"ROR","asserted-by":"publisher"}],"name":"Whitehead Institute for Biomedical Research","place":["Cambridge, United 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Georgia","place":["Athens, United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2041-6295","authenticated-orcid":true,"given":"Silvia NJ","family":"Moreno","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/00te3t702","id-type":"ROR","asserted-by":"publisher"}],"name":"Center for Tropical and Emerging Global Diseases, University of Georgia","place":["Athens, United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5237-1095","authenticated-orcid":true,"given":"Sebastian","family":"Lourido","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/04vqm6w82","id-type":"ROR","asserted-by":"publisher"}],"name":"Whitehead Institute for Biomedical Research","place":["Cambridge, United States"]},{"id":[{"id":"https:\/\/ror.org\/042nb2s44","id-type":"ROR","asserted-by":"publisher"}],"name":"Biology Department, Massachusetts Institute of 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