ArticleMolecular biology of the cell2005
A Plasmodium actin-depolymerizing factor that binds exclusively to actin monomers.
Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 80 citations in OpenAlex.
- Highly divergent apicomplexan cytoskeletons provide additional models for actin biology.The FEBS journal · 2025Review
- Plasmodium actin-like proteins are essential for DNA segregation during male gametogenesis and malaria transmission.PLoS pathogens · 2025Article
- Toxoplasma gondii actin filaments are tuned for rapid disassembly and turnover.Nature communications · 2024Article
- Novel quinolinepiperazinyl-aryltetrazoles targeting the blood stage ofRSC medicinal chemistry · 2024Article
- Article
- Sulfonylpiperazine compounds prevent Plasmodium falciparum invasion of red blood cells through interference with actin-1/profilin dynamics.PLoS biology · 2023Article
- Structure and function of an atypical homodimeric actin capping protein from the malaria parasite.Cellular and molecular life sciences : CMLS · 2022Article
- Recombinant actin-depolymerizing factor of the apicomplexanFrontiers in cellular and infection microbiology · 2022Article
- Inter-subunit interactions drive divergent dynamics in mammalian and Plasmodium actin filaments.PLoS biology · 2018Article
- Apicomplexan actin polymerization depends on nucleation.Scientific reports · 2017Article
- A unique profilin-actin interface is important for malaria parasite motility.PLoS pathogens · 2017Article
- Comparative Plasmodium gene overexpression reveals distinct perturbation of sporozoite transmission by profilin.Molecular biology of the cell · 2016Article
- Expression and identification of the ADF-linker-3-1E gene of Eimeria acervulina of chicken.Parasitology research · 2016Article
- Plasmodium actin is incompletely folded by heterologous protein-folding machinery and likely requires the native Plasmodium chaperonin complex to enter a mature functional state.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2016Article
- Disassembly activity of actin-depolymerizing factor (ADF) is associated with distinct cellular processes in apicomplexan parasites.Molecular biology of the cell · 2015Article
- Towards a molecular understanding of the apicomplexan actin motor: on a road to novel targets for malaria remedies?Acta crystallographica. Section F, Structural biology communications · 2015Review
- The apicomplexan glideosome and adhesins - Structures and function.Journal of structural biology · 2015Review
- Protective efficacy in chickens of recombinant plasmid pET32a(+)-ADF-3-1E of Eimeria acervulina.Parasitology research · 2014Article
- Structural differences explain diverse functions of Plasmodium actins.PLoS pathogens · 2014Article
- A mechanism for actin filament severing by malaria parasite actin depolymerizing factor 1 via a low affinity binding interface.The Journal of biological chemistry · 2014Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ADF/cofilins (AC) are essential F- and G-actin binding proteins that modulate microfilament turnover. The genome of Plasmodium falciparum, the parasite causing malaria, contains two members of the AC family. Interestingly, P. falciparum ADF1 lacks the F-actin binding residues of the AC consensus. Reverse genetics in the rodent malaria model system suggest that ADF1 performs vital functions during the pathogenic red blood cell stages, whereas ADF2 is not present in these stages. We show that recombinant PfADF1 interacts with monomeric actin but does not bind to actin polymers. Although other AC proteins inhibit nucleotide exchange on monomeric actin, the Plasmodium ortholog stimulates nucleotide exchange. Thus, PfADF1 differs in its biochemical properties from previously known AC proteins and seems to promote turnover exclusively by interaction with actin monomers. These findings provide important insights into the low cytosolic abundance and unique turnover characteristics of actin polymers in parasites of the phylum Apicomplexa.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.