Molecular Microbiology
Molecular Microbiology
5 years ago

The serine/threonine phosphatases of apicomplexan parasites

The serine/threonine phosphatases of apicomplexan parasites
Gustavo Arrizabalaga, Chunlin Yang
The balance between phosphorylation and de-phosphorylation, which is delicately regulated by protein kinases and phosphatases, is critical for nearly all biological processes. The Apicomplexa are a large phylum which contains various parasitic protists, including human pathogens, such as Plasmodium, Toxoplasma, Cryptosporidium and Babesia species. The diverse life cycles of these parasites are highly complex and, not surprisingly, many of their key steps are exquisitely regulated by phosphorylation. Interestingly, many of the kinases and phosphatases, as well as the substrates involved in these events are unique to the parasites and therefore phosphorylation constitutes a viable target for antiparasitic intervention. Most progress on this realm has come from studies in Toxoplasma and Plasmodium of their respective kinomes and phosphoproteomes. Nonetheless, given their likely importance, phosphatases have recently become the focus of research within the apicomplexan parasites. In this review, we concentrate on serine/threonine phosphatases in apicomplexan parasites, with the focus on comprehensively identifying and naming protein phosphatases in available apicomplexan genomes, and summarizing the progress of their functional analyses in recent years. The Apicomplexa phylum contains some of the most important pathogenic parasites including Toxoplasma gondii, Plasmodium falciparum, Cryptosporidium parvum and Babesia bovis. Propagation, development, and virulence of these parasites are extensively regulated by phosphorylation and the interplay between kinases and phosphatases. In this review, we catalog and describe the serine/threonine phosphatases of these parasites, which are subdivided into phosphoprotein phosphatases (PPP), protein phosphatases Mg2+/Mn2+ dependent (PPM), and aspartate based phosphatases (FCP/SCP).

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1111/mmi.13715

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