Thrombin receptor ligation and activated rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets

Hartwig, John H.; Bokoch, Gary M.; Carpenter, Christopher L.; Janmey, Paul A.; Taylor, Lance A.; Toker, Alex; Stossel, Thomas P.

doi:10.1016/0092-8674(95)90036-5

Cited by 640 publications

(547 citation statements)

References 43 publications

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“…Among them, polyphosphoinositides are known to play major roles in cellular signalling (reviewed in Payrastre et al, 2001). Small GTPases of the Rho family, RhoA and Rac, are now recognized to be regulators of PI4-P 5-kinase (Chong et al, 1994;Hartwig et al, 1995;Tolias et al, 1995Tolias et al, , 1998Tolias and Cantley, 1999). C3 from C. botulinum, which decreases Rho protein activity, also decreases the cellular level of PIP 2 (Payrastre et al, 2001).…”

Section: Toxins That Modulate Host Polyphosphoinositide Metabolismmentioning

confidence: 99%

Bacterial protein toxins and lipids: role in toxin targeting and activity

Geny

Popoff

2006

Biology of the Cell

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All bacterial toxins, which globally are hydrophilic proteins, interact first with their target cells by recognizing a surface receptor, which is either a lipid or a lipid derivative, or another compound but in a lipid environment. Intracellular active toxins follow various trafficking pathways, the sorting of which is greatly dependent on the nature of the receptor, notably lipidic receptor or receptor embedded into a distinct environment such as lipid microdomains. Numerous other toxins act locally on cell membrane. Indeed, phospholipase activity is a common mechanism shared by several membrane‐damaging toxins. In addition, many toxins active intracellularly or on cell membrane modulate host cell phospholipid pathways. Unusually, a few bacterial toxins require a lipid post‐translational modification to be active. Thereby, lipids are obligate partners of bacterial toxins.

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Section: Toxins That Modulate Host Polyphosphoinositide Metabolismmentioning

confidence: 99%

Bacterial protein toxins and lipids: role in toxin targeting and activity

Geny

Popoff

2006

Biology of the Cell

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“…It has been known for some time that integrins can stimulate the production of Phosphatidyl Inositol biphosphate (PIP 2 ) and recent studies have provided evidence that this e ect is mediated by Rho (Chong et al, 1994;Hartwig et al, 1995), possibly through its interaction with a type I isoform of phosphatidyl inositol 4-phosphate 5-kinase (PIP4-5K) (Ren et al, 1996). The increase in PIP 2 synthesis by Rho A is potentially relevant to focal adhesion assembly because the actin binding activity of several cytoskeletal proteins such as pro®lin and gelsolin is modulated by PIP 2 in vitro (Hartwig et al, 1995) and PIP 2 is enriched in focal adhesion plaques. In light of this, Gilmore and Burridge (1996) reported that the association of PIP 2 with vinculin induces a conformational change in vinculin, allowing it to interact with talin, which binds actin.…”

Section: Role Of Rho Family Of Proteins In Focal Adhesion Assemblymentioning

confidence: 99%

Signaling by integrin receptors

Kumar¹

1998

Oncogene

256

181

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Adhesive interactions are critical for the proliferation, survival and function of all cells. Integrin receptors as the major family of adhesion receptors have been the focus of study for more than a decade. These studies have tremendously enhanced our understanding of the integrin-mediated adhesive interactions and have unraveled novel integrin functions in cell survival mechanisms and in the activation of divergent signaling pathways. The signals from integrin receptors are integrated from those originating from growth factor receptors in order to organize the cytoskeleton, stimulate cell proliferation and rescue cells from matrix detachment-induced programmed cell death. These functions are critical in the regulation of multiple processes such as tissue development, in¯ammation, angiogenesis, tumor cell growth and metastasis and programmed cell death.

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“…The activation of ERM proteins invariably requires PIP2 local accumulation (Hartwig et al 1995;Tolias et al 2000;Honda et al 1999). Two putative binding sites were identified, and PIP2 binding was demonstrated to be essential in guiding ezrin to cell surface locations (Barret et al 2000).…”

Section: Introductionmentioning

confidence: 99%

Ezrin-related Phosphoinositide pathway modifies RhoA and Rac1 in human osteosarcoma cell lines

Vasco

Leopizzi²,

Rocca³

2015

J. Cell Commun. Signal.

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Selected Phosphoinositide-specific Phospholipase C (PI-PLC) enzymes occupy the convergence point of the broad range of pathways that promote Rho and Ras GTPase mediated signalling, which also regulate the activation of ezrin, a member of the ezrin-radixin-moesin (ERM) proteins family involved in the metastatic osteosarcoma spread. Previous studies described that in distinct human osteosarcoma cell lines ezrin networks the PI-PLC with complex interplay controlling the expression of the PLC genes, which codify for PI-PLC enzymes. In the present study, we analyzed the expression and the sub-cellular distribution of RhoA and Rac1 respectively after ezrin silencing and after PI-PLC ε silencing, in order to investigate whether ezrin-RhoGTPAses signalling might involve one or more specific PI-PLC isoforms in cultured 143B and Hs888 human osteosarcoma cell lines. In the present experiments, both ezrin and PLCE gene silencing had different effects upon RhoA and Rac1 expression and subcellular localization. Displacements of Ezrin and of RhoA localization were observed, probably playing functional roles.

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Thrombin receptor ligation and activated rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets

Cited by 640 publications

References 43 publications

Bacterial protein toxins and lipids: role in toxin targeting and activity

Bacterial protein toxins and lipids: role in toxin targeting and activity

Signaling by integrin receptors

Ezrin-related Phosphoinositide pathway modifies RhoA and Rac1 in human osteosarcoma cell lines

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