ArticleMolecular and biochemical parasitology2011
Evidence for prenylation-dependent targeting of a Ykt6 SNARE in Plasmodium falciparum.
Article in Molecular and biochemical parasitology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 23 citations in OpenAlex.
- ELAPOR1 is a copper-dependent tethering factor driving proacrosomal vesicle fusion during acrosome biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Post-Translational Modifications of Proteins of Malaria Parasites during the Life Cycle.International journal of molecular sciences · 2024Review
- Functional screening revealsmBio · 2023Article
- Protein Sorting in Plasmodium Falciparum.Life (Basel, Switzerland) · 2021Review
- ProtozoaDB 2.0: A Trypanosoma Brucei Case Study.Pathogens (Basel, Switzerland) · 2017Article
- The Prenylated Proteome ofMolecular & cellular proteomics : MCP · 2017Article
- Global proteomic analysis of prenylated proteins in Plasmodium falciparum using an alkyne-modified isoprenoid analogue.Scientific reports · 2016Article
- Isoprenoid metabolism in apicomplexan parasites.Current clinical microbiology reports · 2014Article
- Isoprenoid biosynthesis in Plasmodium falciparum.Eukaryotic cell · 2014Review
- Targeting lipid biosynthesis and salvage in apicomplexan parasites for improved chemotherapies.Nature reviews. Microbiology · 2013Review
- Cryptic organelle homology in apicomplexan parasites: insights from evolutionary cell biology.Current opinion in microbiology · 2013Article
- An essential farnesylated kinesin in Trypanosoma brucei.PloS one · 2011Article
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Authors and funding
5 authors at 2 institutions in 1 country.
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Abstract
Ykt6 proteins are the most versatile fusogens in eukaryotic cells, and the only SNAREs that can be both prenylated and acylated at a C-terminal CAAX motif. Unlike yeast and mammalian cells where a single Ykt6 gene is expressed, the Plasmodium falciparum genome encodes two Ykt6 proteins. We have investigated the expression and prenylation of the Ykt6 orthologue, PfYkt6.1 in intra-erythrocytic stages of P. falciparum. PfYkt6.1 localized to the parasite Golgi and other unidentified cytoplasmic compartments, and was partly cytosolic (∼50% in early trophozoites). The membrane-association of PfYkt6.1 was dependent on the presence of a conserved C-terminal CAAX motif (CCSIM). By expressing full-length and mutant proteins in Escherichia coli, we have shown that PfYkt6.1 indeed serves as substrate for prenylation by P. falciparum farnesyltransferases. Surprisingly, PfYkt6.1 could also be geranylgeranylated by parasite extracts independent of the C-terminal amino acid residue. Deletion of the CAAX motif inhibited both farnesylation and geranylgeranylation activities. Additionally, the PfYkt6.1 heptapeptide KQCCSIM, corresponding to the C-terminal CAAX sequence, inhibited the parasite farnesyltransferase activity with an IC(50) of 1 μM. Our findings underscore the importance of CAAX motif-derived peptidomimetics for antimalarial drug development.
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