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The Apicomplexa are a large phylum which contains various parasitic protists, including human pathogens, such as <jats:italic>Plasmodium<\/jats:italic>, <jats:italic>Toxoplasma<\/jats:italic>, <jats:italic>Cryptosporidium<\/jats:italic> and <jats:italic>Babesia<\/jats:italic> 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 <jats:italic>Toxoplasma<\/jats:italic> and <jats:italic>Plasmodium<\/jats:italic> 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.<\/jats:p>","DOI":"10.1111\/mmi.13715","type":"journal-article","created":{"date-parts":[[2017,5,27]],"date-time":"2017-05-27T08:36:38Z","timestamp":1495874198000},"page":"1-21","source":"Crossref","is-referenced-by-count":50,"title":["The serine\/threonine phosphatases of apicomplexan parasites"],"prefix":"10.1111","volume":"106","author":[{"given":"Chunlin","family":"Yang","sequence":"first","affiliation":[{"name":"Department of Pharmacology and Toxicology Indiana University School of Medicine Indianapolis IN 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