ArticlePloS one2012
A unique Kelch domain phosphatase in Plasmodium regulates ookinete morphology, motility and invasion.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- A divergent cyclic nucleotide binding protein promotes Plasmodium ookinete infection of the mosquito.PLoS pathogens · 2025Article
- A subpellicular microtubule dynein transport machinery regulates ookinete morphogenesis for mosquito transmission of Plasmodium yoelii.Nature communications · 2024Article
- Regulators of male and female sexual development are critical for the transmission of a malaria parasite.Cell host & microbe · 2023Article
- Apical anchorage and stabilization of subpellicular microtubules by apical polar ring ensures Plasmodium ookinete infection in mosquito.Nature communications · 2022Article
- Deciphering the Role of Protein Phosphatases in Apicomplexa: The Future of Innovative Therapeutics?Microorganisms · 2022Review
- Functional Characterization of 17 Protein Serine/Threonine Phosphatases inFrontiers in cell and developmental biology · 2021Article
- Zygote morphogenesis but not the establishment of cell polarity in Plasmodium berghei is controlled by the small GTPase, RAB11A.PLoS pathogens · 2020Article
- The serine/threonine phosphatases of apicomplexan parasites.Molecular microbiology · 2017Review
- Rapid inducible protein displacement inWellcome open research · 2017Article
- The development of malaria parasites in the mosquito midgut.Cellular microbiology · 2016Review
- A small mitochondrial protein present in myzozoans is essential for malaria transmission.Open biology · 2016Article
- Transcriptome sequencing and characterization of ungerminated and germinated spores of Nosema bombycis.Acta biochimica et biophysica Sinica · 2016Article
- Conditional Degradation of Plasmodium Calcineurin Reveals Functions in Parasite Colonization of both Host and Vector.Cell host & microbe · 2015Article
- The cell biology of malaria infection of mosquito: advances and opportunities.Cellular microbiology · 2015Review
- Genome wide in silico analysis of Plasmodium falciparum phosphatome.BMC genomics · 2014Article
- The inner membrane complex through development of Toxoplasma gondii and Plasmodium.Cellular microbiology · 2014Review
- PhosphoTyrosyl phosphatase activator of Plasmodium falciparum: identification of its residues involved in binding to and activation of PP2A.International journal of molecular sciences · 2014Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Signalling through post-translational modification (PTM) of proteins is a process central to cell homeostasis, development and responses to external stimuli. The best characterised PTM is protein phosphorylation which is reversibly catalysed at specific residues through the action of protein kinases (addition) and phosphatases (removal). Here, we report characterisation of an orphan protein phosphatase that possesses a domain architecture previously only described in Plantae. Through gene disruption and the production of active site mutants, the enzymatically active Protein Phosphatase containing Kelch-Like domains (PPKL, PBANKA_132950) is shown to play an essential role in the development of an infectious ookinete. PPKL is produced in schizonts and female gametocytes, is maternally inherited where its absence leads to the development of a malformed, immotile, non-infectious ookinete with an extended apical protrusion. The distribution of PPKL includes focussed localization at the ookinete apical tip implying a link between its activity and the correct deployment of the apical complex and microtubule cytoskeleton. Unlike wild type parasites, ppkl(-) ookinetes do not have a pronounced apical distribution of their micronemes yet secretion of microneme cargo is unaffected in the mutant implying that release of microneme cargo is either highly efficient at the malformed apical prominence or secretion may also occur from other points of the parasite, possibly the pellicular pores.
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