ArticleMolecular microbiology2011
Defining the role of a FYVE domain in the localization and activity of a cAMP phosphodiesterase implicated in osmoregulation in Trypanosoma cruzi.
Article in Molecular microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
30 citing papers in PubMed, 51 citations in OpenAlex.
- Cyclic AMP compartmentalization drives signal specificity to control vector colonization and mammalian host infection by American trypanosomes.PLoS pathogens · 2026Article
- Cyclic AMP compartmentalization drives signal specificity to control vector colonization and mammalian host infection by American trypanosomes.bioRxiv : the preprint server for biology · 2025Article
- Outlining the structure of cAMP compartments in Trypanosoma cruzi.Trends in parasitology · 2025Review
- The adhesion plaque mediates fluid discharge and duplication of the contractile vacuole complex in Trypanosoma cruzi.Journal of cell science · 2025Article
- Article
- Adhesion ofmSphere · 2024Article
- Quantitative assessment of the nanoanatomy of the contractile vacuole complex inLife science alliance · 2024Article
- Advances in the cellular biology, biochemistry, and molecular biology of acidocalcisomes.Microbiology and molecular biology reviews : MMBR · 2024Review
- Article
- A sticky situation: When trypanosomatids attach to insect tissues.PLoS pathogens · 2023Review
- Article
- The old and the new about the contractile vacuole of Trypanosoma cruzi.The Journal of eukaryotic microbiology · 2022Review
- New insights into the role of acidocalcisomes in trypanosomatids.The Journal of eukaryotic microbiology · 2022Review
- Perspectives for a new drug candidate for Chagas disease therapy.Memorias do Instituto Oswaldo Cruz · 2022Article
- Signaling pathways involved in environmental sensing in Trypanosoma cruzi.Molecular microbiology · 2021Review
- Tetrahydrophthalazinone Inhibitor of Phosphodiesterase withAntimicrobial agents and chemotherapy · 2021Article
- Efficacy of Novel Pyrazolone Phosphodiesterase Inhibitors in Experimental Mouse Models of Trypanosoma cruzi.Antimicrobial agents and chemotherapy · 2020Article
- Methods to Investigate Signal Transduction Pathways in Trypanosoma cruzi: Cyclic Nucleotide Phosphodiesterases Assay Protocols.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Polyphosphate and acidocalcisomes.Biochemical Society transactions · 2016Review
- cAMP signalling in trypanosomatids: role in pathogenesis and as a drug target.Trends in parasitology · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 7 institutions in 3 countries.
Funding
Abstract
Intracellular levels of cyclic nucleotide second messengers are regulated predominantly by a large superfamily of phosphodiesterases (PDEs). Trypanosoma cruzi, the causative agent of Chagas disease, encodes four different PDE families. One of these PDEs, T. cruzi PDE C2 (TcrPDEC2) has been characterized as a FYVE domain containing protein. Here, we report a novel role for TcrPDEC2 in osmoregulation in T. cruzi and reveal the relevance of its FYVE domain. Our data show that treatment of epimastigotes with TcrPDEC2 inhibitors improves their regulatory volume decrease, whereas cells overexpressing this enzyme are unaffected by the same inhibitors. Consistent with these results, TcrPDEC2 localizes to the contractile vacuole complex, showing strong labelling in the region corresponding to the spongiome. Furthermore, transgenic parasites overexpressing a truncated version of TcrPDEC2 without the FYVE domain show a failure in its targeting to the contractile vacuole complex and a marked decrease in PDE activity, supporting the importance of this domain to the localization and activity of TcrPDEC2. Taking together, the results here presented are consistent with the importance of the cyclic AMP signalling pathway in regulatory volume decrease and implicate TcrPDEC2 as a specifically localized PDE involved in osmoregulation in T. cruzi.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.