ArticleEukaryotic cell2009
Identification and specific localization of tyrosine-phosphorylated proteins in Trypanosoma brucei.
Article in Eukaryotic cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 42 citations in OpenAlex.
- Protein Kinase Inhibitors and Oxidative Stress Modulate In Vivo Phosphorylation ofPharmaceutics · 2026Article
- Key Regulators of Parasite Biology Viewed Through a Post-Translational Modification Repertoire.Proteomics · 2025Review
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- Defeating the trypanosomatid trio: proteomics of the protozoan parasites causing neglected tropical diseases.RSC medicinal chemistry · 2020Review
- Landscapes of Protein Posttranslational Modifications of African Trypanosoma Parasites.iScience · 2020Article
- Unveiling the Kinomes ofComputational and structural biotechnology journal · 2019Article
- Novel Effects of Lapatinib Revealed in the African Trypanosome by Using Hypothesis-Generating Proteomics and Chemical Biology Strategies.Antimicrobial agents and chemotherapy · 2017Article
- New cell motility model observed in parasitic cnidarian Sphaerospora molnari (Myxozoa:Myxosporea) blood stages in fish.Scientific reports · 2016Article
- Differential Subcellular Localization of Leishmania Alba-Domain Proteins throughout the Parasite Development.PloS one · 2015Article
- Quantitative proteomic and phosphoproteomic analysis of Trypanosoma cruzi amastigogenesis.Molecular & cellular proteomics : MCP · 2014Article
- Polo-like kinase phosphorylation of bilobe-resident TbCentrin2 facilitates flagellar inheritance in Trypanosoma brucei.Molecular biology of the cell · 2013Article
- Kinase scaffold repurposing for neglected disease drug discovery: discovery of an efficacious, lapatinib-derived lead compound for trypanosomiasis.Journal of medicinal chemistry · 2013Article
- Global quantitative SILAC phosphoproteomics reveals differential phosphorylation is widespread between the procyclic and bloodstream form lifecycle stages of Trypanosoma brucei.Journal of proteome research · 2013Article
- Identification of a Wee1-like kinase gene essential for procyclic Trypanosoma brucei survival.PloS one · 2013Article
- Article
- Deep evolutionary conservation of an intramolecular protein kinase activation mechanism.PloS one · 2012Article
- The phosphoproteomes of Plasmodium falciparum and Toxoplasma gondii reveal unusual adaptations within and beyond the parasites' boundaries.Cell host & microbe · 2011Article
- Profiling the Trypanosoma cruzi phosphoproteome.PloS one · 2011Article
- Alba-domain proteins of Trypanosoma brucei are cytoplasmic RNA-binding proteins that interact with the translation machinery.PloS one · 2011Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Phosphorylation on tyrosine residues is a key signal transduction mechanism known to regulate intercellular and intracellular communication in multicellular organisms. Despite the lack of conventional tyrosine kinases in the genome of the single cell organism Trypanosoma brucei, phosphorylation on trypanosomal protein tyrosine residues has been reported for this parasite. However, the identities of most of the tyrosine-phosphorylated proteins and their precise site(s) of phosphorylation were unknown. Here, we have applied a phosphotyrosine-specific proteomics approach to identify 34 phosphotyrosine-containing proteins from whole-cell extracts of procyclic form T. brucei. A significant proportion of the phosphotyrosine-containing proteins identified in this study were protein kinases of the CMGC kinase group as well as some proteins of unknown function and proteins involved in energy metabolism, protein synthesis, and RNA metabolism. Interestingly, immunofluorescence microscopy using anti-phosphotyrosine antibodies suggests that there is a concentration of tyrosine-phosphorylated proteins associated with cytoskeletal structures (basal body and flagellum) and in the nucleolus of the parasite. This localization of tyrosine-phosphorylated proteins supports the idea that the function of signaling molecules is controlled by their precise location in T. brucei, a principle well known from higher eukaryotes.
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