ArticleNature communications2016
Export of malaria proteins requires co-translational processing of the PEXEL motif independent of phosphatidylinositol-3-phosphate binding.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- Plasmepsins as Antimalarial Drug Targets-Then, Now, and the Future.Medicinal research reviews · 2026Review
- PfATG18 links V-ATPase assembly to endocytic membrane dynamics in malaria parasites.PLoS pathogens · 2026Article
- An overview of the interconnectedness of the PEXEL and non-PEXEL mediated protein export iniScience · 2025Review
- Proteolytic processing of both RXLR and EER motifs in oomycete effectors.The New phytologist · 2025Article
- APEX2-based proximity proteomic analysis identifies candidate interactors for Plasmodium falciparum knob-associated histidine-rich protein in infected erythrocytes.Scientific reports · 2024Article
- Role of Rabenosyn-5 and Rab5b in host cell cytosol uptake reveals conservation of endosomal transport in malaria parasites.PLoS biology · 2024Article
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- PfEMP1 and var genes - Still of key importance in Plasmodium falciparum malaria pathogenesis and immunity.Advances in parasitology · 2024Review
- Sequence elements within the PEXEL motif and its downstream region modulate PTEX-dependent protein export in Plasmodium falciparum.Traffic (Copenhagen, Denmark) · 2024Article
- The mature N-termini ofmBio · 2023Article
- Article
- Article
- Antiparasitic Effects of Sulfated Polysaccharides from Marine Hydrobionts.Marine drugs · 2021Review
- Artemisinin susceptibility in the malaria parasite Plasmodium falciparum: propellers, adaptor proteins and the need for cellular healing.FEMS microbiology reviews · 2021Review
- Trafficking and Association ofPathogens (Basel, Switzerland) · 2021Article
- Devastating intimacy: the cell biology of plant-Phytophthora interactions.The New phytologist · 2020Review
- Effector prediction and characterization in the oomycete pathogen Bremia lactucae reveal host-recognized WY domain proteins that lack the canonical RXLR motif.PLoS pathogens · 2020Article
- Directing traffic: Chaperone-mediated protein transport in malaria parasites.Cellular microbiology · 2020Review
- The plant-pathogen haustorial interface at a glance.Journal of cell science · 2020Review
Corrections and comments
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Authors and funding
15 authors.
Funding
Abstract
Plasmodium falciparum exports proteins into erythrocytes using the Plasmodium export element (PEXEL) motif, which is cleaved in the endoplasmic reticulum (ER) by plasmepsin V (PMV). A recent study reported that phosphatidylinositol-3-phosphate (PI(3)P) concentrated in the ER binds to PEXEL motifs and is required for export independent of PMV, and that PEXEL motifs are functionally interchangeable with RxLR motifs of oomycete effectors. Here we show that the PEXEL does not bind PI(3)P, and that this lipid is not concentrated in the ER. We find that RxLR motifs cannot mediate export in P. falciparum. Parasites expressing a mutated version of KAHRP, with the PEXEL motif repositioned near the signal sequence, prevented PMV cleavage. This mutant possessed the putative PI(3)P-binding residues but is not exported. Reinstatement of PEXEL to its original location restores processing by PMV and export. These results challenge the PI(3)P hypothesis and provide evidence that PEXEL position is conserved for co-translational processing and export.
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Registered trials
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