<i>Helicobacter pylori</i> toxin VacA induces vacuole formation by acting in the cell cytosol

Bernard, Marina de; Aricò, Beatrice; Papini, Emanuele; Rizzuto, Rosario; Grandi, Guido; Rappuoli, Rino; Montecucco, Cesare

doi:10.1046/j.1365-2958.1997.5881952.x

Cited by 119 publications

(111 citation statements)

References 50 publications

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“…On one hand it is hypothesized that the VacA channel might be formed at the level of the cell plasma membrane and then endocytosed into late endosome to provoke vacuolation (11,12,35). On the other hand, the demonstration that vacuolation could be observed in cells transfected with VacA DNA and expressing the toxin (13,14) has pushed forward the idea that VacA, upon its translocation into the cytosol, could form channels into endomembranes such as those of late endosomes (2,13,14). This latter hypothesis was strengthened by the observation that expression into HeLa cells of a dominant negative mutant of VacA was able to antagonize the cell vacuolation induced by the wild-type toxin also expressed within the cytosol (39,40).…”

Section: Discussionmentioning

confidence: 99%

“…However, it is not clear where the VacA channel is formed in the cell because vacuolation can be induced by intracellular expression of the toxin (2). The toxin may assemble a channel directly at the cell surface (12) or, after endocytosis and translocation into the cytosol, may form a pore in the limiting membrane of intracellular compartments such as late endosomes (13,14). The notion that VacA channel structure and activity observed in artificial lipid bilayers (8 -11) might be similar to those found in living cells (11,12) has been also challenged recently (15).…”

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confidence: 99%

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Glycosylphosphatidylinositol-anchored Proteins and Actin Cytoskeleton Modulate Chloride Transport by Channels Formed by the Helicobacter pylori Vacuolating Cytotoxin VacA in HeLa Cells

Gauthier

Ricci

Gounon

et al. 2004

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Glycosylphosphatidylinositol-anchored Proteins and Actin Cytoskeleton Modulate Chloride Transport by Channels Formed by the Helicobacter pylori Vacuolating Cytotoxin VacA in HeLa Cells

Gauthier

Ricci

Gounon

et al. 2004

Journal of Biological Chemistry

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“…Vaccinia virus stock was trypsinized at 37°C for 30 min with vigorous vortexing every 5-10 min, and then 10 l was added to HeLa cells (de Bernard et al, 1997). After infection for 30 min at 37°C, the virus stock was removed, and HeLa cells were transfected with pCDNA3-myc-hrs or the pCDNA3 vector.…”

Section: Cell Culture and Transfectionmentioning

confidence: 99%

CART: An Hrs/Actinin-4/BERP/Myosin V Protein Complex Required for Efficient Receptor Recycling

Yan

Wei

Kujala

et al. 2005

MBoC

114

121

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Altering the number of surface receptors can rapidly modulate cellular responses to extracellular signals. Some receptors, like the transferrin receptor (TfR), are constitutively internalized and recycled to the plasma membrane. Other receptors, like the epidermal growth factor receptor (EGFR), are internalized after ligand binding and then ultimately degraded in the lysosome. Routing internalized receptors to different destinations suggests that distinct molecular mechanisms may direct their movement. Here, we report that the endosome-associated protein hrs is a subunit of a protein complex containing actinin-4, BERP, and myosin V that is necessary for efficient TfR recycling but not for EGFR degradation. The hrs/actinin-4/BERP/myosin V (CART [cytoskeleton-associated recycling or transport]) complex assembles in a linear manner and interrupting binding of any member to its neighbor produces an inhibition of transferrin recycling rate. Disrupting the CART complex results in shunting receptors to a slower recycling pathway that involves the recycling endosome. The novel CART complex may provide a molecular mechanism for the actin-dependence of rapid recycling of constitutively recycled plasma membrane receptors. INTRODUCTIONEndocytosis is required for the uptake of essential nutrients from the extracellular environment as well as for retrieval of proteins and lipids that are added to the plasma membrane during fusion of regulated and constitutive secretory vesicles (De Camilli and Takei, 1996;Koenig and Ikeda, 1996;Robinson et al., 1996;Mukherjee et al., 1997;Schmid, 1997;Betz and Angleson, 1998;Koenig et al., 1998;Stoorvogel, 1998;D'Hondt et al., 2000;Gruenberg, 2001). The endocytic pathway can be separated into numerous stages based on the movement of cargo and the identification of morphologically defined compartments (De Camilli and Takei, 1996;Koenig and Ikeda, 1996;Robinson et al., 1996;Mukherjee et al., 1997;Schmid, 1997;Betz and Angleson, 1998;Koenig et al., 1998;Stoorvogel, 1998;D'Hondt et al., 2000;Gruenberg, 2001). Early events in the endocytic process include membrane invagination and vesicle budding from the plasma membrane, formation of transport vesicles, and fusion with early endosomes. Later events include cargo sorting, and additional transport/fusion steps, including those responsible for transport to the lysosome for degradation, and those responsible for recycling back to various compartments (De Camilli and Takei, 1996;Koenig and Ikeda, 1996;Robinson et al., 1996;Mukherjee et al., 1997;Schmid, 1997;Betz and Angleson, 1998;Koenig et al., 1998;Stoorvogel, 1998;D'Hondt et al., 2000;Gruenberg, 2001). Although much progress has been made in elucidating the molecular processes involved in early endocytic events, such as those involved in the genesis of clathrin-coated endocytic transport vesicles, an equally clear understanding of later events remains elusive.The early endosome is a crucial point in the endocytic pathway to sort cargo for transport to late endosomes for eventual degradation in the...

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“…Release-There is substantial evidence that VacA associates with and enters mammalian cells to elaborate an intracellular activity resulting in vacuolation (44,(47)(48)(49)(50)(51). Notably, the entry of VacA into target cells is facilitated by activation, which consists of briefly exposing the toxin to acidic pH (44).…”

Section: Activation Of Vaca Is Important For Toxin-mediated Mitochondmentioning

confidence: 99%

Cellular Vacuolation and Mitochondrial Cytochrome c Release Are Independent Outcomes of Helicobacter pylori Vacuolating Cytotoxin Activity That Are Each Dependent on Membrane Channel Formation

Willhite

Cover²,

Blanke³

2003

Journal of Biological Chemistry

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Helicobacter pylori toxin VacA induces vacuole formation by acting in the cell cytosol

Cited by 119 publications

References 50 publications

Glycosylphosphatidylinositol-anchored Proteins and Actin Cytoskeleton Modulate Chloride Transport by Channels Formed by the Helicobacter pylori Vacuolating Cytotoxin VacA in HeLa Cells

Glycosylphosphatidylinositol-anchored Proteins and Actin Cytoskeleton Modulate Chloride Transport by Channels Formed by the Helicobacter pylori Vacuolating Cytotoxin VacA in HeLa Cells

CART: An Hrs/Actinin-4/BERP/Myosin V Protein Complex Required for Efficient Receptor Recycling

Cellular Vacuolation and Mitochondrial Cytochrome c Release Are Independent Outcomes of Helicobacter pylori Vacuolating Cytotoxin Activity That Are Each Dependent on Membrane Channel Formation

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