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Post‐translational modifications as key regulators of apicomplexan biology: insights from proteome‐wide studies
Author(s) -
Yakubu Rama R.,
Weiss Louis M.,
Silmon de Monerri Natalie C.
Publication year - 2018
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.13867
Subject(s) - biology , proteome , crosstalk , acetylation , computational biology , model organism , microbiology and biotechnology , glycosylation , posttranslational modification , apicomplexa , protozoa , plasmodium falciparum , genetics , biochemistry , gene , immunology , physics , optics , enzyme , malaria
Summary Parasites of the Apicomplexa phylum, such as Plasmodium spp. and Toxoplasma gondii , undergo complex life cycles involving multiple stages with distinct biology and morphologies. Post‐translational modifications (PTMs), such as phosphorylation, acetylation and glycosylation, regulate numerous cellular processes, playing a role in every aspect of cell biology. PTMs can occur on proteins at any time in their lifespan and through alterations of target protein activity, localization, protein–protein interactions, among other functions, dramatically increase proteome diversity and complexity. In addition, PTMs can be induced or removed on changes in cellular environment and state. Thus, PTMs are likely to be key regulators of developmental transitions, biology and pathogenesis of apicomplexan parasites. In this review we examine the roles of PTMs in both parasite‐specific and conserved eukaryotic processes, and the potential crosstalk between PTMs, that together regulate the intricate lives of these protozoa.