ArticleBMC genomics2007
The TriTryp phosphatome: analysis of the protein phosphatase catalytic domains.
Article in BMC genomics, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 98 citations in OpenAlex.
- Beyond the catalysis of Trypanosoma cruzi trans-sialidases: structure, function, post-translational modifications, intrinsically disordered regions and use of CRISPR/Cas9.Archives of microbiology · 2026Review
- Key Regulators of Parasite Biology Viewed Through a Post-Translational Modification Repertoire.Proteomics · 2025Review
- Functional Characterization of MIP_07528 ofBiology · 2025Article
- Development of a 2,4-Diaminothiazole Series for the Treatment of Human African Trypanosomiasis Highlights the Importance of Static-Cidal Screening of Analogues.Journal of medicinal chemistry · 2023Article
- Knockout of protein phosphatase 1 in Leishmania major reveals its role during RNA polymerase II transcription termination.Nucleic acids research · 2023Article
- Structure, function and druggability of the African trypanosome flagellum.Journal of cellular physiology · 2022Review
- Delineating transitions during the evolution of specialised peroxisomes: Glycosome formation in kinetoplastid and diplonemid protists.Frontiers in cell and developmental biology · 2022Article
- In Silico Characterization of Calcineurin from Pathogenic Obligate Intracellular Trypanosomatids: Potential New Biological Roles.Biomolecules · 2021Article
- Parasite protein phosphatases: biological function, virulence, and host immune evasion.Parasitology research · 2021Review
- Protein Serine/Threonine Phosphatase Type 2C ofFrontiers in cellular and infection microbiology · 2021Article
- Protein Phosphatase PP2C Identification inBioMed research international · 2021Article
- TheFrontiers in cellular and infection microbiology · 2021Article
- Identification of a novel base J binding protein complex involved in RNA polymerase II transcription termination in trypanosomes.PLoS genetics · 2020Article
- Article
- Measurement of Acid Ecto-phosphatase Activity in LiveBio-protocol · 2019Article
- Identification of Functional and Druggable Sites inInternational journal of molecular sciences · 2019Article
- Quantitative phosphoproteome and proteome analyses emphasize the influence of phosphorylation events during the nutritional stress of Trypanosoma cruzi: the initial moments of in vitro metacyclogenesis.Cell stress & chaperones · 2019Article
- Reprogramming of Trypanosoma cruzi metabolism triggered by parasite interaction with the host cell extracellular matrix.PLoS neglected tropical diseases · 2019Article
- Identification of TOEFAZ1-interacting proteins reveals key regulators of Trypanosoma brucei cytokinesis.Molecular microbiology · 2018Article
- Non-linear hierarchy of the quorum sensing signalling pathway in bloodstream form African trypanosomes.PLoS pathogens · 2018Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
backgroundThe genomes of the three parasitic protozoa Trypanosoma cruzi, Trypanosoma brucei and Leishmania major are the main subject of this study. These parasites are responsible for devastating human diseases known as Chagas disease, African sleeping sickness and cutaneous Leishmaniasis, respectively, that affect millions of people in the developing world. The prevalence of these neglected diseases results from a combination of poverty, inadequate prevention and difficult treatment. Protein phosphorylation is an important mechanism of controlling the development of these kinetoplastids. With the aim to further our knowledge of the biology of these organisms we present a characterisation of the phosphatase complement (phosphatome) of the three parasites.
resultsAn ontology-based scan of the three genomes was used to identify 86 phosphatase catalytic domains in T. cruzi, 78 in T. brucei, and 88 in L. major. We found interesting differences with other eukaryotic genomes, such as the low proportion of tyrosine phosphatases and the expansion of the serine/threonine phosphatase family. Additionally, a large number of atypical protein phosphatases were identified in these species, representing more than one third of the total phosphatase complement. Most of the atypical phosphatases belong to the dual-specificity phosphatase (DSP) family and show considerable divergence from classic DSPs in both the domain organisation and sequence features.
conclusionThe analysis of the phosphatome of the three kinetoplastids indicates that they possess orthologues to many of the phosphatases reported in other eukaryotes, including humans. However, novel domain architectures and unusual combinations of accessory domains, suggest distinct functional roles for several of the kinetoplastid phosphatases, which await further experimental exploration. These distinct traits may be exploited in the selection of suitable new targets for drug development to prevent transmission and spread of the diseases, taking advantage of the already extensive knowledge on protein phosphatase inhibitors.
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