The serine/threonine phosphatases of apicomplexan parasites. Issue 1 (14th June 2017)
- Record Type:
- Journal Article
- Title:
- The serine/threonine phosphatases of apicomplexan parasites. Issue 1 (14th June 2017)
- Main Title:
- The serine/threonine phosphatases of apicomplexan parasites
- Authors:
- Yang, Chunlin
Arrizabalaga, Gustavo - Abstract:
- 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. Abstract : The Apicomplexa phylum contains some of the most important pathogenic parasites including Toxoplasma gondii, Plasmodium falciparum, Cryptosporidium parvum and Babesia bovis . Propagation, development, andSummary: 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. Abstract : 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 Mg 2+/ Mn 2+ dependent (PPM), and aspartate based phosphatases (FCP/SCP). … (more)
- Is Part Of:
- Molecular microbiology. Volume 106:Issue 1(2017)
- Journal:
- Molecular microbiology
- Issue:
- Volume 106:Issue 1(2017)
- Issue Display:
- Volume 106, Issue 1 (2017)
- Year:
- 2017
- Volume:
- 106
- Issue:
- 1
- Issue Sort Value:
- 2017-0106-0001-0000
- Page Start:
- 1
- Page End:
- 21
- Publication Date:
- 2017-06-14
- Subjects:
- Molecular microbiology -- Periodicals
572.829 - Journal URLs:
- http://www.blackwell-synergy.com/servlet/useragent?func=showIssues&code=mmi&close=2003#C2003 ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1365-2958 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/mmi.13715 ↗
- Languages:
- English
- ISSNs:
- 0950-382X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5900.817960
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 4685.xml