Interaction of Enteropathogenic or Enterohemorrhagic
            <i>Escherichia coli</i>
            with HeLa Cells Results in Translocation of Cortactin to the Bacterial Adherence Site

Cantarelli, Vlademir Vicente; Takahashi, Akira; Akeda, Yukihiro; Nagayama, Kenichi; Honda, Takeshi

doi:10.1128/iai.68.1.382-386.2000

Cited by 43 publications

(48 citation statements)

References 19 publications

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“…In most cell types cortactin localizes in cytoplasmic punctate structures of unknown composition concentrated at the perinuclear region, and also with F-actin at sites of dynamic peripherial membrane activity (Figure 3a,b). Cortactin translocates from the cytoplasm to the periphery in response to many of the same stimuli that induce its tyrosine phosphorylation, including growth factor treatment, integrin activation and bacterial entry (Ozawa et al, 1995;Weed et al, 1998;Cantarelli et al, 2000). These events also lead to activation of Rac (Hartwig et al, 1995;Clark et al, 1998;Mounier et al, 1999), which together with Cdc42 are responsible for controlling the formation of cortical actin networks (Ridley et al, 1992;Kozma et al, 1995).…”

Section: The Role Of Cortactin In Cortical Actin Organizationmentioning

confidence: 99%

Cortactin: coupling membrane dynamics to cortical actin assembly

2001

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Exposure of cells to a variety of external signals causes rapid changes in plasma membrane morphology. Plasma membrane dynamics, including membrane ru e and microspike formation, fusion or ®ssion of intracellular vesicles, and the spatial organization of transmembrane proteins, is directly controlled by the dynamic reorganization of the underlying actin cytoskeleton. Two members of the Rho family of small GTPases, Cdc42 and Rac, have been well established as mediators of extracellular signaling events that impact cortical actin organization. Actin-based signaling through Cdc42 and Rac ultimately results in activation of the actin-related protein (Arp) 2/3 complex, which promotes the formation of branched actin networks. In addition, the activity of both receptor and non-receptor protein tyrosine kinases along with numerous actin binding proteins works in concert with Arp2/3-mediated actin polymerization in regulating the formation of dynamic cortical actin-associated structures. In this review we discuss the structure and role of the cortical actin binding protein cortactin in Rho GTPase and tyrosine kinase signaling events, with the emphasis on the roles cortactin plays in tyrosine phosphorylation-based signal transduction, regulating cortical actin assembly, transmembrane receptor organization and membrane dynamics. We also consider how aberrant regulation of cortactin levels contributes to tumor cell invasion and metastasis. Oncogene (2001) 20, 6418 ± 6434.

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Section: The Role Of Cortactin In Cortical Actin Organizationmentioning

confidence: 99%

Cortactin: coupling membrane dynamics to cortical actin assembly

2001

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“…Interference of WASP with dominantnegative constructs or cells lacking N-WASP prevents pedestal formation (Kalman et al, 1999;Lommel et al, 2001). Interestingly, cortactin, which binds and activates the Arp2/3 complex, is directly recruited to TIR, and dominant-negative mutants of cortactin block F-actin accumulation beneath the attached bacteria (Cantarelli et al, 2000;Cantarelli et al, 2002).…”

Section: Lessons From Phagocytosismentioning

confidence: 99%

Coupling membrane protrusion and cell adhesion

DeMali

Burridge

2003

Journal of Cell Science

170

141

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The ability of cells to extend cell membranes is central to numerous biological processes, including cell migration, cadherin-mediated junction formation and phagocytosis. Much attention has been focused on understanding the signals that trigger membrane protrusion and the architecture of the resulting extension. Similarly, cell adhesion has been extensively studied,yielding a wealth of information about the proteins involved and how they signal to the cytoplasm. Although we have learned much about membrane protrusion and cell adhesion, we know less about how these two processes are coupled. Traditionally it has been thought that they are linked by the signaling pathways they employ – for example, those involving Rho family GTPases. However, there are also physical links between the cellular machineries that mediate cell adhesion and membrane protrusion, such as vinculin.

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“…For example, NcK, a mammalian adaptor protein implicated in the initiation of actin signaling, binds to the 12-amino-acid sequence surrounding the tyrosine-phosphorylated Y474 residue of Tir (19,76) and is essential for lesion formation. Additionally, vinculin (58), cortactin (20,21), talin (21,58), and ␣-actinin (58, 75) all interact directly with Tir, and the last three are required for the organization of the actin pedestal. Since Tir spans the membrane and since vinculin, talin, ␣-actinin, and many of the other cytoskeletal proteins found in the pedestal are all also components of focal adhesion plaques, it has been postulated that Tir might be acting in a manner similar to that of an ␤ 1 -integrin (73).…”

Section: Epec Secreted Proteinsmentioning

confidence: 99%

Virulence of EnteropathogenicEscherichia coli, a Global Pathogen

et al. 2003

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Enteropathogenic Escherichia coli (EPEC) remains an important cause of diarrheal disease worldwide. Research into EPEC is intense and provides a good virulence model of other E. coli infections as well as other pathogenic bacteria. Although the virulence mechanisms are now better understood, they are extremely complex and much remains to be learnt. The pathogenesis of EPEC depends on the formation of an ultrastructural lesion in which the bacteria make intimate contact with the host apical enterocyte membrane. The formation of this lesion is a consequence of the ability of EPEC to adhere in a localized manner to the host cell, aided by bundle-forming pili. Tyrosine phosphorylation and signal transduction events occur within the host cell at the lesion site, leading to a disruption of the host cell mechanisms and, consequently, to diarrhea. These result from the action of highly regulated EPEC secreted proteins which are released via a type III secretion system, many genes of which are located within a pathogenicity island known as the locus of enterocyte effacement. Over the last few years, dramatic increases in our knowledge of EPEC virulence have taken place. This review therefore aims to provide a broad overview of and update to the virulence aspects of EPEC

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Interaction of Enteropathogenic or Enterohemorrhagic Escherichia coli with HeLa Cells Results in Translocation of Cortactin to the Bacterial Adherence Site

Abstract: Infection of cultured HeLa epithelial cells with enteropathogenic

Cited by 43 publications

References 19 publications

Cortactin: coupling membrane dynamics to cortical actin assembly

Cortactin: coupling membrane dynamics to cortical actin assembly

Coupling membrane protrusion and cell adhesion

Virulence of EnteropathogenicEscherichia coli, a Global Pathogen

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