ArticlePLoS pathogens2008
Repetitive N-WASP-binding elements of the enterohemorrhagic Escherichia coli effector EspF(U) synergistically activate actin assembly.
Article in PLoS pathogens, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 51 citations in OpenAlex.
- Cytoskeletal mechanisms regulating attaching/effacing bacteria interactions with host cells: It takes a village to build the pedestal.BioEssays : news and reviews in molecular, cellular and developmental biology · 2024Review
- Why put yourself on a pedestal? The pathogenic role of the A/E pedestal.Infection and immunity · 2024Review
- Branching out in different directions: Emerging cellular functions for the Arp2/3 complex and WASP-family actin nucleation factors.European journal of cell biology · 2023Article
- Emerging Concepts in Defective Macrophage Phagocytosis in Cystic Fibrosis.International journal of molecular sciences · 2022Review
- A teamwork promotion of formin-mediated actin nucleation by Bud6 and Aip5 inMolecular biology of the cell · 2022Article
- Enteropathogenic E. coli relies on collaboration between the formin mDia1 and the Arp2/3 complex for actin pedestal biogenesis and maintenance.PLoS pathogens · 2018Article
- CRISPR Screen Reveals that EHEC's T3SS and Shiga Toxin Rely on Shared Host Factors for Infection.mBio · 2018Article
- Extracellular motility and cell-to-cell transmission of enterohemorrhagic E. coli is driven by EspFU-mediated actin assembly.PLoS pathogens · 2017Article
- Why should cell biologists study microbial pathogens?Molecular biology of the cell · 2015Article
- Wash functions downstream of Rho1 GTPase in a subset of Drosophila immune cell developmental migrations.Molecular biology of the cell · 2015Article
- The ability of an attaching and effacing pathogen to trigger localized actin assembly contributes to virulence by promoting mucosal attachment.Cellular microbiology · 2014Article
- Intimate host attachment: enteropathogenic and enterohaemorrhagic Escherichia coli.Cellular microbiology · 2013Review
- A bacterial encoded protein induces extreme multinucleation and cell-cell internalization in intestinal cells.Tissue barriers · 2013Article
- Actin cytoskeleton manipulation by effector proteins secreted by diarrheagenic Escherichia coli pathotypes.BioMed research international · 2013Review
- Insights into the pathogenesis of enteropathogenic E. coli using an improved intestinal enterocyte model.PloS one · 2013Article
- Enteropathogenic Escherichia coli and vaccinia virus do not require the family of WASP-interacting proteins for pathogen-induced actin assembly.Infection and immunity · 2012Article
- Membrane-deforming proteins play distinct roles in actin pedestal biogenesis by enterohemorrhagic Escherichia coli.The Journal of biological chemistry · 2012Article
- Pathogens and polymers: microbe-host interactions illuminate the cytoskeleton.The Journal of cell biology · 2011Review
- Bacterial subversion of host actin dynamics at the plasma membrane.Cellular microbiology · 2011Review
- The EHEC type III effector NleL is an E3 ubiquitin ligase that modulates pedestal formation.PloS one · 2011Article
Corrections and comments
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Authors and funding
10 authors at 5 institutions in 2 countries.
Funding
Abstract
Enterohemorrhagic Escherichia coli (EHEC) generate F-actin-rich adhesion pedestals by delivering effector proteins into mammalian cells. These effectors include the translocated receptor Tir, along with EspF(U), a protein that associates indirectly with Tir and contains multiple peptide repeats that stimulate actin polymerization. In vitro, the EspF(U) repeat region is capable of binding and activating recombinant derivatives of N-WASP, a host actin nucleation-promoting factor. In spite of the identification of these important bacterial and host factors, the underlying mechanisms of how EHEC so potently exploits the native actin assembly machinery have not been clearly defined. Here we show that Tir and EspF(U) are sufficient for actin pedestal formation in cultured cells. Experimental clustering of Tir-EspF(U) fusion proteins indicates that the central role of the cytoplasmic portion of Tir is to promote clustering of the repeat region of EspF(U). Whereas clustering of a single EspF(U) repeat is sufficient to bind N-WASP and generate pedestals on cultured cells, multi-repeat EspF(U) derivatives promote actin assembly more efficiently. Moreover, the EspF(U) repeats activate a protein complex containing N-WASP and the actin-binding protein WIP in a synergistic fashion in vitro, further suggesting that the repeats cooperate to stimulate actin polymerization in vivo. One explanation for repeat synergy is that simultaneous engagement of multiple N-WASP molecules can enhance its ability to interact with the actin nucleating Arp2/3 complex. These findings define the minimal set of bacterial effectors required for pedestal formation and the elements within those effectors that contribute to actin assembly via N-WASP-Arp2/3-mediated signaling pathways.
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Registered trials
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.