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Global analysis of apicomplexan protein S-acyl transferases reveals an enzyme essential for invasion
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2013 (English)In: Traffic: the International Journal of Intracellular Transport, ISSN 1398-9219, E-ISSN 1600-0854, Vol. 14, no 8, p. 895-911Article in journal (Refereed) Published
Abstract [en]

The advent of techniques to study palmitoylation on a whole proteome scale has revealed that it is an important reversible modification that plays a role in regulating multiple biological processes. Palmitoylation can control the affinity of a protein for lipid membranes, which allows it to impact protein trafficking, stability, folding, signalling and interactions. The publication of the palmitome of the schizont stage of Plasmodium falciparum implicated a role for palmitoylation in host cell invasion, protein export and organelle biogenesis. However, nothing is known so far about the repertoire of protein S-acyl transferases (PATs) that catalyse this modification in Apicomplexa. We undertook a comprehensive analysis of the repertoire of Asp-His-His-Cys cysteine-rich domain (DHHC-CRD) PAT family in Toxoplasma gondii and Plasmodium berghei by assessing their localization and essentiality. Unlike functional redundancies reported in other eukaryotes, some apicomplexan-specific DHHCs are essential for parasite growth, and several are targeted to organelles unique to this phylum. Of particular interest is DHHC7, which localizes to rhoptry organelles in all parasites tested, including the major human pathogen P. falciparum. TgDHHC7 interferes with the localization of the rhoptry palmitoylated protein TgARO and affects the apical positioning of the rhoptry organelles. This PAT has a major impact on T. gondii host cell invasion, but not on the parasite's ability to egress.

Place, publisher, year, edition, pages
John Wiley & Sons, 2013. Vol. 14, no 8, p. 895-911
Keywords [en]
Apicomplexa, egress, invasion, palmitoyl acyl transferase, palmitoylation, Plasmodium berghei, Plasmodium falciparum, rhoptry organelle, Toxoplasma gondii
National Category
Cell and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-165863DOI: 10.1111/tra.12081ISI: 000321434400003PubMedID: 23638681OAI: oai:DiVA.org:umu-165863DiVA, id: diva2:1379125
Funder
Wellcome trust, WT098051Available from: 2019-12-16 Created: 2019-12-16 Last updated: 2019-12-18Bibliographically approved

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