ArticleThe Journal of biological chemistry2013
Identification of biochemically distinct properties of the small ubiquitin-related modifier (SUMO) conjugation pathway in Plasmodium falciparum.
Article in The Journal of biological chemistry, 2013. 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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Who cites it
15 citing papers in PubMed.
- UBA2: the gatekeeper of the sumoylation pathway and its multifaceted roles in human diseases and therapeutic prospects.Clinical and experimental medicine · 2026Review
- Key Regulators of Parasite Biology Viewed Through a Post-Translational Modification Repertoire.Proteomics · 2025Review
- Population genetic analysis of Plasmodium knowlesi reveals differential selection and exchange events between Borneo and Peninsular sub-populations.Scientific reports · 2023Article
- Implications of critical node-dependent unidirectional cross-talk of Plasmodium SUMO pathway proteins.Biophysical journal · 2022Article
- SUMOylation in Phytopathogen Interactions: Balancing Invasion and Resistance.Frontiers in cell and developmental biology · 2021Review
- Targeting SUMOylation inFrontiers in cellular and infection microbiology · 2021Review
- Characterization of Plasmodium falciparum NEDD8 and identification of cullins as its substrates.Scientific reports · 2020Article
- Ubiquitin-Like Modifiers: Emerging Regulators of Protozoan Parasites.Biomolecules · 2020Review
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- Comparative Time-Scale Gene Expression Analysis Highlights the Infection Processes of TwoFrontiers in microbiology · 2018Article
- Post-translational modifications as key regulators of apicomplexan biology: insights from proteome-wide studies.Molecular microbiology · 2018Review
- Structural analysis and evolution of specificity of the SUMO UFD E1-E2 interactions.Scientific reports · 2017Article
- Characterization and Structural Insights into Selective E1-E2 Interactions in the Human and Plasmodium falciparum SUMO Conjugation Systems.The Journal of biological chemistry · 2016Article
- The ubiquitin system: an essential component to unlocking the secrets of malaria parasite biology.Molecular bioSystems · 2014Review
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Small ubiquitin-related modifiers (SUMOs) are post-translationally conjugated to other proteins and are thereby essential regulators of a wide range of cellular processes. Sumoylation, and enzymes of the sumoylation pathway, are conserved in the malaria causing parasite, Plasmodium falciparum. However, the specific functions of sumoylation in P. falciparum, and the degree of functional conservation between enzymes of the human and P. falciparum sumoylation pathways, have not been characterized. Here, we demonstrate that sumoylation levels peak during midstages of the intra-erythrocyte developmental cycle, concomitant with hemoglobin consumption and elevated oxidative stress. In vitro studies revealed that P. falciparum E1- and E2-conjugating enzymes interact effectively to recognize and modify RanGAP1, a model mammalian SUMO substrate. However, in heterologous reactions, P. falciparum E1 and E2 enzymes failed to interact with cognate human E2 and E1 partners, respectively, to modify RanGAP1. Structural analysis, binding studies, and functional assays revealed divergent amino acid residues within the E1-E2 binding interface that define organism-specific enzyme interactions. Our studies identify sumoylation as a potentially important regulator of oxidative stress response during the P. falciparum intra-erythrocyte developmental cycle, and define E1 and E2 interactions as a promising target for development of parasite-specific inhibitors of sumoylation and parasite replication.
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