Palmitoylation in apicomplexan parasites: from established regulatory roles to putative new functions.
Corvi, M. M. and Turowski, V. R.
Laboratorio de Bioquimica y Biologia Celular de Parasitos, Instituto Tecnologico de Chascomus (INTECH), CONICET, Universidad Nacional de San Martin. Intendente Marino Km 8.2, B7130, Chascomus, Buenos Aires, Argentina. Electronic address: mcorvi@intech.gov.ar.
Laboratorio de Bioquimica y Biologia Celular de Parasitos, Instituto Tecnologico de Chascomus (INTECH), CONICET, Universidad Nacional de San Martin. Intendente Marino Km 8.2, B7130, Chascomus, Buenos Aires, Argentina.
This minireview aims to provide a comprehensive synthesis on protein palmitoylation in apicomplexan parasites and higher eukaryotes where most of the data is available. Apicomplexan parasites encompass numerous obligate intracellular parasites with significant health risk to animals and humans. Protein palmitoylation is a widespread post-translational modification that plays important regulatory roles in several physiological and pathological states. Functional studies demonstrate that many processes important for parasites are regulated by protein palmitoylation. Structural analyses suggest that enzymes responsible for the palmitoylation process have a conserved architecture in eukaryotes although there are particular differences which could be related to their substrate specificities. Interestingly, with the publication of T. gondii and P. falciparum palmitoylomes new possible regulatory functions are unveiled. Here we focus our discussion on data from both palmitoylomes that suggest that palmitoylation of nuclear proteins regulate different chromatin-related processes such as nucleosome assembly and stability, transcription, translation and DNA repair.
Molecular and Biochemical Parasitology 230: 16-23 (2019)