Asset Details
Do you wish to reserve the book?
Temporal and thermal profiling of the Toxoplasma proteome implicates parasite Protein Phosphatase 1 in the regulation of Ca2+-responsive pathways
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Temporal and thermal profiling of the Toxoplasma proteome implicates parasite Protein Phosphatase 1 in the regulation of Ca2+-responsive pathways
Do you wish to request the book?
Temporal and thermal profiling of the Toxoplasma proteome implicates parasite Protein Phosphatase 1 in the regulation of Ca2+-responsive pathways
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Temporal and thermal profiling of the Toxoplasma proteome implicates parasite Protein Phosphatase 1 in the regulation of Ca2+-responsive pathways
2022
Overview
Apicomplexan parasites cause persistent mortality and morbidity worldwide through diseases including malaria, toxoplasmosis, and cryptosporidiosis. Ca 2+ 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 2+ -responsive proteins, little is known about how specific signaling elements interact to impact pathogenesis. We mapped the Ca 2+ -responsive proteome of the model apicomplexan Taxoplasma gondii via time-resolved phosphoproteomics and thermal proteome profiling. The waves of phosphoregulation following PKG activation and stimulated Ca 2+ release corroborate known physiological changes but identify specific proteins operating in these pathways. Thermal profiling of parasite extracts identified many expected Ca 2+ -responsive proteins, such as parasite Ca 2+ -dependent protein kinases. Our approach also identified numerous Ca 2+ -responsive proteins that are not predicted to bind Ca 2+ , yet are critical components of the parasite signaling network. We characterized protein phosphatase 1 (PP1) as a Ca 2+ -responsive enzyme that relocalized to the parasite apex upon Ca 2+ store release. Conditional depletion of PP1 revealed that the phosphatase regulates Ca 2+ uptake to promote parasite motility. PP1 may thus be partly responsible for Ca 2+ -regulated serine/threonine phosphatase activity in apicomplexan parasites.
Publisher
eLife Sciences Publications Ltd,eLife Sciences Publications, Ltd
