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The serine/threonine phosphatases of apicomplexan parasites
Author(s) -
Yang Chunlin,
Arrizabalaga Gustavo
Publication year - 2017
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.13715
Subject(s) - biology , phosphorylation , kinase , phosphatase , apicomplexa , serine , protein phosphorylation , plasmodium (life cycle) , cryptosporidium parvum , biochemistry , threonine , microbiology and biotechnology , protein kinase a , plasmodium falciparum , parasite hosting , immunology , malaria , world wide web , computer science
Summary 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.

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