ArticleProceedings of the National Academy of Sciences of the United States of America1998
Compartmentation of phosphoglycerate kinase in Trypanosoma brucei plays a critical role in parasite energy metabolism.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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30 citing papers in PubMed, 92 citations in OpenAlex.
- Profile of lysine acetylation in Eimeria tenella and its potential implications for anticoccidial research.Parasites & vectors · 2026Article
- Several different sequences are implicated in bloodstream-form-specific gene expression in Trypanosoma brucei.PLoS neglected tropical diseases · 2022Article
- Divergent metabolism between Trypanosoma congolense and Trypanosoma brucei results in differential sensitivity to metabolic inhibition.PLoS pathogens · 2021Article
- Potential therapeutic targets shared between leishmaniasis and cancer.Parasitology · 2021Review
- Phosphoglycerate kinase: structural aspects and functions, with special emphasis on the enzyme from Kinetoplastea.Open biology · 2020Review
- The phosphoinositide regulatory network in Trypanosoma brucei: Implications for cell-wide regulation in eukaryotes.PLoS neglected tropical diseases · 2020Review
- An immunoproteomic approach to identifying immunoreactive proteins inPathogens and global health · 2019Article
- Proteomic analysis of glycosomes from Trypanosoma cruzi epimastigotes.Molecular and biochemical parasitology · 2019Article
- The suppressive cap-binding complex factor 4EIP is required for normal differentiation.Nucleic acids research · 2018Article
- Inositol polyphosphate multikinase regulation of Trypanosoma brucei life stage development.Molecular biology of the cell · 2018Article
- Expression of the RNA-binding protein RBP10 promotes the bloodstream-form differentiation state in Trypanosoma brucei.PLoS pathogens · 2017Article
- Article
- Eukaryotic translation elongation factor-1 alpha is associated with a specific subset of mRNAs in Trypanosoma cruzi.BMC microbiology · 2015Article
- Contribution of pyruvate phosphate dikinase in the maintenance of the glycosomal ATP/ADP balance in the Trypanosoma brucei procyclic form.The Journal of biological chemistry · 2014Article
- A genome-wide tethering screen reveals novel potential post-transcriptional regulators in Trypanosoma brucei.PLoS pathogens · 2014Article
- Evidence for loss of a partial flagellar glycolytic pathway during trypanosomatid evolution.PloS one · 2014Article
- Explicit consideration of topological and parameter uncertainty gives new insights into a well-established model of glycolysis.The FEBS journal · 2013Article
- Role of cytosolic glyceraldehyde-3-phosphate dehydrogenase in visceral organ infection by Leishmania donovani.Eukaryotic cell · 2013Article
- Leishmania amazonensis arginase compartmentalization in the glycosome is important for parasite infectivity.PloS one · 2012Article
- Immunobiology of African trypanosomes: need of alternative interventions.Journal of biomedicine & biotechnology · 2010Article
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4 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
African trypanosomes compartmentalize glycolysis in a microbody, the glycosome. When growing in the mammalian bloodstream, trypanosomes contain only a rudimentary mitochondrion, and the first seven glycolytic enzymes, including phosphoglycerate kinase, are located in the glycosome. Procyclic trypanosomes, growing in the gut of tsetse flies, possess a fully developed mitochondrion that is active in oxidative phosphorylation. The first six glycolytic enzymes are still glycosomal, but phosphoglycerate kinase is now found in the cytosol. We demonstrate here that bloodstream trypanosomes are killed by expression of cytosolic phosphoglycerate kinase. The toxicity depends on both enzyme activity and cytosolic location. One possible explanation is that cytosolic phosphoglycerate kinase creates an ATP-generating shunt in the cytosol, thus preventing full ATP regeneration in the glycosome and ultimately inhibiting the first, ATP-consuming, steps of glycolysis.
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