biostudies-literatureFrenal KHoward Hughes Medical InstituteMedical Research CouncilWellcome Trust895-911https://www.ebi.ac.uk/biostudies/studies/S-EPMC3813974biostudies-literatureUnknown14(8)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) PATTraffic (Copenhagen, Denmark)Global analysis of apicomplexan protein S-acyl transferases reveals an enzyme essential for invasion.PMC3813974G0501670)G0501670WT098051Rayner JCBushell ESFrenal KTay CLJia YGraindorge ASoldati-Favre DMueller CBillker OfalseGlobal analysis of apicomplexan protein S-acyl transferases reveals an enzyme essential for invasion.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) PAT2013-01-01T00:00:00Z2013 Aug2026-05-01T21:18:04.937Z2019-03-27T01:17:53ZS-EPMC38139742363868110.1111/tra.12081