EspFU Is a Translocated EHEC Effector that Interacts with Tir and N-WASP and Promotes Nck-Independent Actin Assembly
Open Access
- 1 August 2004
- journal article
- research article
- Published by Elsevier in Developmental Cell
- Vol. 7 (2) , 217-228
- https://doi.org/10.1016/j.devcel.2004.07.004
Abstract
No abstract availableKeywords
This publication has 36 references indexed in Scilit:
- Clustering of Nck by a 12-residue Tir phosphopeptide is sufficient to trigger localized actin assemblyThe Journal of cell biology, 2004
- The Murine Nck SH2/SH3 Adaptors Are Important for the Development of Mesoderm-Derived Embryonic Structures and for Regulating the Cellular Actin NetworkMolecular and Cellular Biology, 2003
- Tails of two Tirs: actin pedestal formation by enteropathogenic E. coli and enterohemorrhagic E. coli O157:H7Current Opinion in Microbiology, 2003
- Genetic Engineering Using Homologous RecombinationAnnual Review of Genetics, 2002
- A tyrosine‐phosphorylated 12‐amino‐acid sequence of enteropathogenic Escherichia coli Tir binds the host adaptor protein Nck and is required for Nck localization to actin pedestalsMolecular Microbiology, 2002
- Enterohaemorrhagic and enteropathogenic Escherichia coli use a different Tir‐based mechanism for pedestal formationMolecular Microbiology, 2001
- Role of EspF in host cell death induced by enteropathogenic Escherichia coliCellular Microbiology, 2001
- Pathogenesis and evolution of virulence in enteropathogenic and enterohemorrhagic Escherichia coliJournal of Clinical Investigation, 2001
- Enteropathogenic Escherichia coli (EPEC) attachment to epithelial cells: exploiting the host cell cytoskeleton from the outsideCellular Microbiology, 2000
- EspE, a novel secreted protein of attaching and effacing bacteria, is directly translocated into infected host cells, where it appears as a tyrosine‐phosphorylated 90 kDa proteinMolecular Microbiology, 1998