Journal
MOLECULAR AND BIOCHEMICAL PARASITOLOGY
Volume 207, Issue 1, Pages 39-44Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molbiopara.2016.03.011
Keywords
Toxoplasma gondii; Apicoplast; Phosphoinositides; Pleckstrin Homology domain; PI(3,5)P-2
Categories
Funding
- FRM (Fondation pour la Recherche Medicale)
- Laboratoire d'Excellence (LabEx) [ParaFrapANR-11-LABX-0024]
- Fondation pour la Recherche Medicale (Equipe FRM) [DEQ20130326508]
- ANR API-COPIP [ANR 11 BSV3 015 01]
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The phosphoinositide phosphatidylinositol-3,5-bisphosphate (PI(3,5)P-2) plays crucial roles in the maintenance of lysosomeivacuole morphology, membrane trafficking and regulation of endolysosome-localized membrane channel activity. In Toxoplasma gondii, we previously reported that PI(3,5)P-2 is essential for parasite survival by controlling homeostasis of the apicoplast, a particular organelle of algal origin. Here, by using a phosphoinositide pull-down assay, we identified TgPH1 in Toxoplasma a protein conserved in many apicomplexan parasites. TgPH1 binds specifically to PI(3,5)P-2, shows punctate intracellular localization, but plays no vital role for tachyzoite growth in vitro. TgPH1 is a protein predominantly formed by a pleckstrin homology (PH) domain. So far, PH domains have been described to bind preferentially to bis- or trisphosphate phosphoinositides containing two adjacent phosphates (i.e. PI(3,4)P-2, PI(4,5)P-2, PI(3,4,5)P3). Therefore, our study reveals an unusual feature of TgPH1 which binds preferentially to Pl(3,5)P-2. (C) 2016 Elsevier B.V. All rights reserved.
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