ArticleMolecular & cellular proteomics : MCP2011
SUMOylation pathway in Trypanosoma cruzi: functional characterization and proteomic analysis of target proteins.
Article in Molecular & cellular proteomics : MCP, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 53 citations in OpenAlex.
- An Overview ofPathogens (Basel, Switzerland) · 2025Review
- Targeting RNA-binding proteins with small molecules: perspectives and challenges.Frontiers in chemistry · 2025Review
- Ubiquitin-Like Modifiers: Emerging Regulators of Protozoan Parasites.Biomolecules · 2020Review
- Defeating the trypanosomatid trio: proteomics of the protozoan parasites causing neglected tropical diseases.RSC medicinal chemistry · 2020Review
- Ubiquitination and the Proteasome as Drug Targets in Trypanosomatid Diseases.Frontiers in chemistry · 2020Review
- Identification ofFrontiers in endocrinology · 2019Article
- High-throughput Methods for Dissection of Trypanosome Gene Regulatory Networks.Current genomics · 2018Review
- SUMO polymeric chains are involved in nuclear foci formation and chromatin organization in Trypanosoma brucei procyclic forms.PloS one · 2018Article
- Characterization and Diagnostic Application of Trypanosoma cruzi Trypomastigote Excreted-Secreted Antigens Shed in Extracellular Vesicles Released from Infected Mammalian Cells.Journal of clinical microbiology · 2017Article
- Regulation of RNA binding proteins in trypanosomatid protozoan parasites.World journal of biological chemistry · 2016Review
- Identification of enzymes involved in SUMOylation in Trypanosoma brucei.Scientific reports · 2015Article
- SUMO proteomics to decipher the SUMO-modified proteome regulated by various diseases.Proteomics · 2015Review
- Biosynthesis of SUMOylated Proteins in Bacteria Using the Trypanosoma brucei Enzymatic System.PloS one · 2015Article
- SUMOylation by the E3 ligase TbSIZ1/PIAS1 positively regulates VSG expression in Trypanosoma brucei.PLoS pathogens · 2014Article
- Deletion of ubiquitin fold modifier protein Ufm1 processing peptidase Ufsp in L. donovani abolishes Ufm1 processing and alters pathogenesis.PLoS neglected tropical diseases · 2014Article
- SUMOylation in Trypanosoma brucei.PeerJ · 2013Article
- Deletion of mitochondrial associated ubiquitin fold modifier protein Ufm1 in Leishmania donovani results in loss of β-oxidation of fatty acids and blocks cell division in the amastigote stage.Molecular microbiology · 2012Article
- Regulation of the cell division cycle in Trypanosoma brucei.Eukaryotic cell · 2012Review
- Antagonic activities of Trypanosoma cruzi metacaspases affect the balance between cell proliferation, death and differentiation.Cell death and differentiation · 2012Article
- SUMOylation in Giardia lamblia: A Conserved Post-Translational Modification in One of the Earliest Divergent Eukaryotes.Biomolecules · 2012Article
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Authors and funding
10 authors at 6 institutions in 4 countries.
Funding
Abstract
SUMOylation is a relevant protein post-translational modification in eukaryotes. The C terminus of proteolytically activated small ubiquitin-like modifier (SUMO) is covalently linked to a lysine residue of the target protein by an isopeptide bond, through a mechanism that includes an E1-activating enzyme, an E2-conjugating enzyme, and transfer to the target, sometimes with the assistance of a ligase. The modification is reversed by a protease, also responsible for SUMO maturation. A number of proteins have been identified as SUMO targets, participating in the regulation of cell cycle progression, transcription, translation, ubiquitination, and DNA repair. In this study, we report that orthologous genes corresponding to the SUMOylation pathway are present in the etiological agent of Chagas disease, Trypanosoma cruzi. Furthermore, the SUMOylation system is functionally active in this protozoan parasite, having the requirements for SUMO maturation and conjugation. Immunofluorescence analysis showed that T. cruzi SUMO (TcSUMO) is predominantly found in the nucleus. To identify SUMOylation targets and get an insight into their physiological roles we generated transfectant T. cruzi epimastigote lines expressing a double-tagged T. cruzi SUMO, and SUMOylated proteins were enriched by tandem affinity chromatography. By two-dimensional liquid chromatography-mass spectrometry a total of 236 proteins with diverse biological functions were identified as potential T. cruzi SUMO targets. Of these, metacaspase-3 was biochemically validated as a bona fide SUMOylation substrate. Proteomic studies in other organisms have reported that orthologs of putative T. cruzi SUMOylated proteins are similarly modified, indicating conserved functions for protein SUMOylation in this early divergent eukaryote.
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