ArticlePLoS pathogens2014
EhCoactosin stabilizes actin filaments in the protist parasite Entamoeba histolytica.
Article in PLoS pathogens, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 28 citations in OpenAlex.
- The cytoskeleton of pathogenic protists.Bioscience reports · 2026Review
- AGC family kinase of Entamoeba histolytica: Decoding the members biochemically.PLoS pathogens · 2024Article
- Article
- Coactosin-like protein 1 regulates integrity and repair of model intestinal epithelial barriers via actin binding dependent and independent mechanisms.Frontiers in cell and developmental biology · 2024Article
- Editorial: Vesicular transport, the actin cytoskeleton and their involvement in virulence mechanisms during host-parasite interaction.Frontiers in cellular and infection microbiology · 2023Article
- Comparative transcriptome profiling of virulent and avirulent isolates of Neoparamoeba perurans.Scientific reports · 2022Article
- Unravelling the Biology of EhActo as the First Cofilin FromFrontiers in cell and developmental biology · 2022Article
- Calcium modulates the domain flexibility and function of an α-actinin similar to the ancestral α-actinin.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- EhC2B, a C2 domain-containing protein, promotes erythrophagocytosis in Entamoeba histolytica via actin nucleation.PLoS pathogens · 2020Article
- Surface Plasmon Resonance Analysis of the Protein-protein Binding Specificity Using Autolab ESPIRIT.Bio-protocol · 2020Article
- Uncovering the Cyclic AMP Signaling Pathway of the Protozoan ParasiteFrontiers in cellular and infection microbiology · 2020Article
- EhP3, a homolog of 14-3-3 family of protein participates in actin reorganization and phagocytosis in Entamoeba histolytica.PLoS pathogens · 2019Article
- Morphodynamics of the Actin-Rich Cytoskeleton inFrontiers in cellular and infection microbiology · 2018Article
- AGC family kinase 1 participates in trogocytosis but not in phagocytosis in Entamoeba histolytica.Nature communications · 2017Article
- Cofilin-1 and Other ADF/Cofilin Superfamily Members in Human Malignant Cells.International journal of molecular sciences · 2016Review
- Proteomic Identification of Oxidized Proteins in Entamoeba histolytica by Resin-Assisted Capture: Insights into the Role of Arginase in Resistance to Oxidative Stress.PLoS neglected tropical diseases · 2016Article
- The Entamoeba histolytica, Arp2/3 Complex Is Recruited to Phagocytic Cups through an Atypical Kinase EhAK1.PLoS pathogens · 2015Article
- Crystal structure of calcium binding protein-5 from Entamoeba histolytica and its involvement in initiation of phagocytosis of human erythrocytes.PLoS pathogens · 2014Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Entamoeba histolytica is a protist parasite that is the causative agent of amoebiasis, and is a highly motile organism. The motility is essential for its survival and pathogenesis, and a dynamic actin cytoskeleton is required for this process. EhCoactosin, an actin-binding protein of the ADF/cofilin family, participates in actin dynamics, and here we report our studies of this protein using both structural and functional approaches. The X-ray crystal structure of EhCoactosin resembles that of human coactosin-like protein, with major differences in the distribution of surface charges and the orientation of terminal regions. According to in vitro binding assays, full-length EhCoactosin binds both F- and G-actin. Instead of acting to depolymerize or severe F-actin, EhCoactosin directly stabilizes the polymer. When EhCoactosin was visualized in E. histolytica cells using either confocal imaging or total internal reflectance microscopy, it was found to colocalize with F-actin at phagocytic cups. Over-expression of this protein stabilized F-actin and inhibited the phagocytic process. EhCoactosin appears to be an unusual type of coactosin involved in E. histolytica actin dynamics.
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