ArticleInternational journal of molecular sciences2014
PhosphoTyrosyl phosphatase activator of Plasmodium falciparum: identification of its residues involved in binding to and activation of PP2A.
Article in International journal of molecular sciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 14 citations in OpenAlex.
- Article
- From Genes to Transcripts, a Tightly Regulated Journey inFrontiers in cellular and infection microbiology · 2020Review
- The role of epigenetics and chromatin structure in transcriptional regulation in malaria parasites.Briefings in functional genomics · 2019Review
- Plasmodium pseudo-Tyrosine Kinase-like binds PP1 and SERA5 and is exported to host erythrocytes.Scientific reports · 2019Article
- Prediction of Signal Peptides in Proteins from Malaria Parasites.International journal of molecular sciences · 2018Article
- Calcium-binding proteins that are type B″ regulatory subunits of phosphatase 2A in Giardia intestinalis.Parasitology research · 2018Article
- Changes in genome organization of parasite-specific gene families during the Plasmodium transmission stages.Nature communications · 2018Article
- Characterization of a Protein Phosphatase Type-1 and a Kinase Anchoring Protein inFrontiers in microbiology · 2018Article
- The serine/threonine phosphatases of apicomplexan parasites.Molecular microbiology · 2017Review
- Identification of Plasmodium falciparum Translation Initiation eIF2β Subunit: Direct Interaction with Protein Phosphatase Type 1.Frontiers in microbiology · 2016Article
- Genome wide in silico analysis of Plasmodium falciparum phosphatome.BMC genomics · 2014Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Plasmodium falciparum (Pf), the causative agent of the deadliest form of malaria, a tight regulation of phosphatase activity is crucial for the development of the parasite. In this study, we have identified and characterized PfPTPA homologous to PhosphoTyrosyl Phosphatase Activator, an activator of protein phosphatase 2A which is a major phosphatase involved in many biological processes in eukaryotic cells. The PfPTPA sequence analysis revealed that five out of six amino acids involved in interaction with PP2A in human are conserved in P. falciparum. Localization studies showed that PfPTPA and PfPP2A are present in the same compartment of blood stage parasites, suggesting a possible interaction of both proteins. In vitro binding and functional studies revealed that PfPTPA binds to and activates PP2A. Mutation studies showed that three residues (V(283), G(292) and M(296)) of PfPTPA are indispensable for the interaction and that the G(292) residue is essential for its activity. In P. falciparum, genetic studies suggested the essentiality of PfPTPA for the completion of intraerythrocytic parasite lifecycle. Using Xenopus oocytes, we showed that PfPTPA blocked the G2/M transition. Taken together, our data suggest that PfPTPA could play a role in the regulation of the P. falciparum cell cycle through its PfPP2A regulatory activity.
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