ArticleProceedings of the National Academy of Sciences of the United States of America2011
Minimal requirements for actin filament disassembly revealed by structural analysis of malaria parasite actin-depolymerizing factor 1.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Highly divergent apicomplexan cytoskeletons provide additional models for actin biology.The FEBS journal · 2025Review
- Sulfonylpiperazine compounds prevent Plasmodium falciparum invasion of red blood cells through interference with actin-1/profilin dynamics.PLoS biology · 2023Article
- Recombinant actin-depolymerizing factor of the apicomplexanFrontiers in cellular and infection microbiology · 2022Article
- Identification and characterisation of a phospholipid scramblase in the malaria parasite Plasmodium falciparum.Molecular and biochemical parasitology · 2021Article
- The Ringleaders: Understanding the Apicomplexan Basal Complex Through Comparison to Established Contractile Ring Systems.Frontiers in cellular and infection microbiology · 2021Review
- Actomyosin forces and the energetics of red blood cell invasion by the malaria parasite Plasmodium falciparum.PLoS pathogens · 2020Article
- 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
- Feisty filaments: actin dynamics in the red blood cell membrane skeleton.Current opinion in hematology · 2016Review
- 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
- Localisation-based imaging of malarial antigens during erythrocyte entry reaffirms a role for AMA1 but not MTRAP in invasion.Journal of cell science · 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
- The apicomplexan glideosome and adhesins - Structures and function.Journal of structural biology · 2015Review
- Pivotal and distinct role for Plasmodium actin capping protein alpha during blood infection of the malaria parasite.Molecular microbiology · 2015Article
- Solution structures and dynamics of ADF/cofilins UNC-60A and UNC-60B from Caenorhabditis elegans.The Biochemical journal · 2015Article
- 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
- The exported protein PbCP1 localises to cleft-like structures in the rodent malaria parasite Plasmodium berghei.PloS one · 2013Article
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16 authors.
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Abstract
Malaria parasite cell motility is a process that is dependent on the dynamic turnover of parasite-derived actin filaments. Despite its central role, actin's polymerization state is controlled by a set of identifiable regulators that is markedly reduced compared with those of other eukaryotic cells. In Plasmodium falciparum, the most virulent species that affects humans, this minimal repertoire includes two members of the actin-depolymerizing factor/cofilin (AC) family of proteins, P. falciparum actin-depolymerizing factor 1 (PfADF1) and P. falciparum actin-depolymerizing factor 2. This essential class of actin regulator is involved in the control of filament dynamics at multiple levels, from monomer binding through to filament depolymerization and severing. Previous biochemical analyses have suggested that PfADF1 sequesters monomeric actin but, unlike most eukaryotic counterparts, has limited potential to bind or depolymerize filaments. The molecular basis for these unusual properties and implications for parasite cell motility have not been established. Here we present the crystal structure of an apicomplexan AC protein, PfADF1. We show that PfADF1 lacks critical residues previously implicated as essential for AC-mediated actin filament binding and disassembly, having a substantially reduced filament-binding loop and C-terminal α4 helix. Despite this divergence in structure, we demonstrate that PfADF1 is capable of efficient actin filament severing. Furthermore, this severing occurs despite PfADF1's low binding affinity for filaments. Comparative structural analysis along with biochemical and microscopy evidence establishes that severing is reliant on the availability of an exposed basic residue in the filament-binding loop, a conserved minimal requirement that defines AC-mediated filament disassembly across eukaryotic cells.
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