ArticleParasitology research2008
Protein phosphatase 5 is required for Hsp90 function during proteotoxic stresses in Trypanosoma brucei.
Article in Parasitology research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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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.
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Who cites it
15 citing papers in PubMed, 25 citations in OpenAlex.
- Hsp90 and associates shaping parasite biology.mSphere · 2025Review
- Hsp90, a team player in protein quality control and the stress response in bacteria.Microbiology and molecular biology reviews : MMBR · 2024Review
- Tackling Sleeping Sickness: Current and Promising Therapeutics and Treatment Strategies.International journal of molecular sciences · 2023Review
- Article
- Cytosolic and Mitochondrial Hsp90 in Cytokinesis, Mitochondrial DNA Replication, and Drug Action in Trypanosoma brucei.Antimicrobial agents and chemotherapy · 2021Article
- Parasite protein phosphatases: biological function, virulence, and host immune evasion.Parasitology research · 2021Review
- Plasmodium berghei serine/threonine protein phosphatase PP5 plays a critical role in male gamete fertility.International journal for parasitology · 2019Article
- Prediction of Protein Complexes inMolecular & cellular proteomics : MCP · 2017Article
- Characterizing heat shock protein 90 gene of Apolygus lucorum (Meyer-Dür) and its expression in response to different temperature and pesticide stresses.Cell stress & chaperones · 2014Article
- Trypanosome alternative oxidase possesses both an N-terminal and internal mitochondrial targeting signal.Eukaryotic cell · 2014Article
- Catalytic activity of a novel serine/threonine protein phosphatase PP5 from Leishmania major.Parasite (Paris, France) · 2014Article
- Potent antitrypanosomal activities of heat shock protein 90 inhibitors in vitro and in vivo.The Journal of infectious diseases · 2013Article
- Trypanosomatid protein phosphatases.Molecular and biochemical parasitology · 2010Review
- PPEF/PP7 protein Ser/Thr phosphatases.Cellular and molecular life sciences : CMLS · 2009Review
- Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms.Cell stress & chaperones · 2009Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Trypanosoma brucei, a parasitic protozoan that causes African trypanosomiasis in human and domestic animals, adapt in various environments during their digenetic life cycle. In this study, we found that Hsp90 is crucial for the survival of this parasite. Inhibition of Hsp90 activity by geldanamycin (GA) reduced cell growth and increased the level of Hsp90. Both the bloodstream and procyclic forms of T. brucei showed a several-fold greater sensitivity than the mammalian cells to GA and also to 17-AAG, a less toxic derivative of GA, suggesting that Hsp90 could be a potential chemotherapeuric target for African trypanosomiasis. T. brucei Hsp90 interacts with the protein phosphatase 5 (PP5) in vivo. Under normal growth conditions, T. brucei PP5 (TbPP5) and Hsp90 are primarily localized in the cytosol. However, with increase in growth temperature and GA treatment, these proteins translocate to the nucleus. Overproduction of TbPP5 by genetic manipulation reduced the growth inhibitory effect of GA, while knockdown of TbPP5 reduced cell growth more in the presence of GA, as compared to parental control. Depletion of TbPP5, however, did not prevent the induction of Hsp90 protein level during GA treatment. Together, these results suggest that TbPP5 positively regulates the function of Hsp90 to maintain cellular homeostasis during proteotoxic stresses in T. brucei.
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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.