Journal article
An apically located hybrid guanylate cyclase-ATPase is critical for the initiation of Ca2 signaling and motility in Toxoplasma gondii
L Yang, AD Uboldi, S Seizova, ML Wilde, MJ Coffey, NJ Katris, Y Yamaryo-Botté, M Kocan, RAD Bathgate, RJ Stewart, MJ McConville, PE Thompson, CY Botté, CJ Tonkin
Journal of Biological Chemistry | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 2019
Open access
Abstract
Protozoan parasites of the phylum Apicomplexa actively move through tissue to initiate and perpetuate infection. The regulation of parasite motility relies on cyclic nucleotide-dependent kinases, but how these kinases are activated remains unknown. Here, using an array of biochemical and cell biology approaches, we show that the apicomplexan parasite Toxoplasma gondii expresses a large guanylate cyclase (TgGC) protein, which contains several upstream ATPase transporter-like domains. We show that TgGC has a dynamic localization, being concentrated at the apical tip in extracellular parasites, which then relocates to a more cytosolic distribution during intracellular replication. Conditional T..
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Awarded by State Government of Victoria
Funding Acknowledgements
This work was supported by Australian Research Council (ARC) Future Fellowship FT120100164 (to C.J.T.); a China Council scholarship (to L.Y.); Victorian State Government Operational Infrastructure Support and the Australian Government National Health and Medical Research Council (NHMRC) Independent Medical Research Institutes Infrastructure Support Scheme (IRIISS); Agence Nationale de la Recherche, France Grant ANR-12-PDOC-0028-Project Apicolipid, the Atip-Avenir and Finovi programs (CNRS-INSERM-FinoviAtip-Avenir Apicolipid projects), and Laboratoire d' Excellence Parafrap, France Grant ANR-11-LABX-0024 (to C.Y.B., Y.Y.-B., and N.J.K.); the Laboratoire International Associe (LIA) CNRS Program (Apicolipid project) (to C.Y.B. and C.J.T.); and an NHMR Cprinciple research fellowship (to M.J.M.).