ArticlePloS one2014
Plasmodium falciparum Rab5B is an N-terminally myristoylated Rab GTPase that is targeted to the parasite's plasma and food vacuole membranes.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 35 citations in OpenAlex.
- Role of Rabenosyn-5 and Rab5b in host cell cytosol uptake reveals conservation of endosomal transport in malaria parasites.PLoS biology · 2024Article
- Phylogenetic reconstruction and evolution of the Rab GTPase gene family in Amoebozoa.Small GTPases · 2022Article
- Inhibition of protein N-myristoylation blocks Plasmodium falciparum intraerythrocytic development, egress and invasion.PLoS biology · 2021Article
- Artemisinin susceptibility in the malaria parasite Plasmodium falciparum: propellers, adaptor proteins and the need for cellular healing.FEMS microbiology reviews · 2021Review
- Emerging Mechanisms of Endocytosis inLife (Basel, Switzerland) · 2021Review
- ThemBio · 2020Article
- Rab5b-Associated Arf1 GTPase Regulates Export of N-Myristoylated Adenylate Kinase 2 From the Endoplasmic Reticulum inFrontiers in cellular and infection microbiology · 2020Article
- Genome-wide scan reveals genetic divergence and diverse adaptive selection in Chinese local cattle.BMC genomics · 2019Article
- Druggable Targets in Cyclic Nucleotide Signaling Pathways in Apicomplexan Parasites and Kinetoplastids against Disabling Protozoan Diseases in Humans.International journal of molecular sciences · 2019Review
- Dynamic protein S-palmitoylation mediates parasite life cycle progression and diverse mechanisms of virulence.Critical reviews in biochemistry and molecular biology · 2017Review
- The Prenylated Proteome ofMolecular & cellular proteomics : MCP · 2017Article
- Host cell remodeling by pathogens: the exomembrane system in Plasmodium-infected erythrocytes.FEMS microbiology reviews · 2016Review
- Rab5 Isoforms Specifically Regulate Different Modes of Endocytosis in Leishmania.The Journal of biological chemistry · 2016Article
- Plasmodium Rab5b is secreted to the cytoplasmic face of the tubovesicular network in infected red blood cells together with N-acylated adenylate kinase 2.Malaria journal · 2016Article
- Identification and characterization of a member of Rab subfamily, Rab8, from Clonorchis sinensis.Parasitology research · 2015Article
- Article
- Malaria Parasite-Infected Erythrocytes Secrete PfCK1, the Plasmodium Homologue of the Pleiotropic Protein Kinase Casein Kinase 1.PloS one · 2015Article
- Resolving the homology-function relationship through comparative genomics of membrane-trafficking machinery and parasite cell biology.Molecular and biochemical parasitologyReview
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Authors and funding
14 authors at 5 institutions in 4 countries.
Funding
Abstract
Plasmodium falciparum (Pf) has a family of 11 Rab GTPases to regulate its vesicular transport. However, PfRab5B is unique in lacking a C-terminal geranyl-geranylation motif, while having N-terminal palmitoylation and myristoylation motifs. We show that the N-terminal glycine is required for PfRab5B myristoylation in vitro and when an N-terminal PfRab5B fragment possessing both acylation motifs is fused to GFP and expressed in transgenic P. falciparum parasites, the chimeric PfRab5B protein localizes to the plasma membrane. Upon substitution of the modified glycine by alanine the staining becomes diffuse and GFP is found in soluble subcellular fractions. Immuno-electron microscopy shows endogenous PfRab5B decorating the parasite's plasma and food vacuole membranes. Using reverse genetics rab5b couldn't be deleted from the haploid genome of asexual blood stage P. berghei parasites. The failure of PbRab5A or PbRab5C to complement for loss of PbRab5B function indicates non-overlapping roles for the three Plasmodium Rab5s, with PfRab5B involved in trafficking MSP1 to the food vacuole membrane and CK1 to the plasma membrane. We discuss similarities between Plasmodium Rab5B and Arabidopsis thaliana ARA6, a similarly unusual Rab5-like GTPase of plants.
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