ArticleThe Journal of biological chemistry2011
Crystal structures explain functional differences in the two actin depolymerization factors of the malaria parasite.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 34 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
- 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
- Cofilin Acts as a Booster for Progression of Malignant Tumors Represented by Glioma.Cancer management and research · 2022Review
- An actin-depolymerizing factor from the halophyte smooth cordgrass, Spartina alterniflora (SaADF2), is superior to its rice homolog (OsADF2) in conferring drought and salt tolerance when constitutively overexpressed in rice.Plant biotechnology journal · 2019Article
- 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
- Computational Study of the Binding Mechanism of Actin-Depolymerizing Factor 1 with Actin in Arabidopsis thaliana.PloS one · 2016Article
- Disassembly activity of actin-depolymerizing factor (ADF) is associated with distinct cellular processes in apicomplexan parasites.Molecular biology of the cell · 2015Article
- Plasmodium falciparum coronin organizes arrays of parallel actin filaments potentially guiding directional motility in invasive malaria parasites.Malaria journal · 2015Article
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- 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
- EhCoactosin stabilizes actin filaments in the protist parasite Entamoeba histolytica.PLoS pathogens · 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
- Mammalian and malaria parasite cyclase-associated proteins catalyze nucleotide exchange on G-actin through a conserved mechanism.The Journal of biological chemistry · 2013Article
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Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Apicomplexan parasites, such as the malaria-causing Plasmodium, utilize an actin-based motor for motility and host cell invasion. The actin filaments of these parasites are unusually short, and actin polymerization is under strict control of a small set of regulatory proteins, which are poorly conserved with their mammalian orthologs. Actin depolymerization factors (ADFs) are among the most important actin regulators, affecting the rates of filament turnover in a multifaceted manner. Plasmodium has two ADFs that display low sequence homology with each other and with the higher eukaryotic family members. Here, we show that ADF2, like canonical ADF proteins but unlike ADF1, binds to both globular and filamentous actin, severing filaments and inducing nucleotide exchange on the actin monomer. The crystal structure of Plasmodium ADF1 shows major differences from the ADF consensus, explaining the lack of F-actin binding. Plasmodium ADF2 structurally resembles the canonical members of the ADF/cofilin family.
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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.