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Protein Disulfide Isomerase Acts as a Redox-Dependent Chaperone to Unfold Cholera Toxin
It is shown that protein disulfide isomerase (PDI) in the ER lumen functions to disassemble and unfold the toxin once its A chain has been cleaved, indicating that PDI can act as a novel type of chaperone, whose binding and release of substrates is regulated by a redox, rather than an ATPase, cycle. Expand
Gangliosides are receptors for murine polyoma virus and SV40
It is demonstrated that specific gangliosides can serve as plasma membrane receptors for these viruses, GD1a and GT1b for Py and GM1 for SV40, and binding and flotation assays were used to show that addition of these gangLiosides to phospholipid vesicles allowed specific binding of the respective viruses. Expand
Human neonatal Fc receptor mediates transport of IgG into luminal secretions for delivery of antigens to mucosal dendritic cells.
It is found that the human neonatal Fc receptor (FcRn) is the vehicle that transports IgG across the intestinal epithelial barrier into the lumen where the IgG can bind cognate antigen. Expand
Myosin light chain phosphorylation regulates barrier function by remodeling tight junction structure
It is concluded that myosin light chain phosphorylation alone is sufficient to induce tight junction regulation and new insights are provided into the molecular mechanisms that mediate this regulation. Expand
The intracellular voyage of cholera toxin: going retro.
Cholera toxin (CT) and related AB(5)-subunit toxins move from the plasma membrane through the trans-Golgi and endoplasmic reticulum (ER) to the cytosol of host cells. The toxins exploit a specificExpand
Bidirectional FcRn-dependent IgG transport in a polarized human intestinal epithelial cell line.
A novel bidirectional mechanism of IgG transport across epithelial barriers that predicts an important effect of FcRn on IgG function in immune surveillance and host defense at mucosal surfaces is defined. Expand
Targeting of cholera toxin and Escherichia coli heat labile toxin in polarized epithelia: role of COOH-terminal KDEL
Evidence is provided that CT and LT interact directly with endogenous KDEL-receptors and imply that both toxins may require retrograde movement through Golgi cisternae and ER for efficient and maximal biologic activity. Expand
Cholera Toxin: An Intracellular Journey into the Cytosol by Way of the Endoplasmic Reticulum
The mechanisms of toxin trafficking by GM1 and retro-translocation of the A1-chain to the cytosol are reviewed and ADP-ribosylating the large G-protein Gs and activating adenylyl cyclase are reviewed. Expand
Derlin-1 facilitates the retro-translocation of cholera toxin.
It is demonstrated that a dominant-negative Derlin-1-YFP fusion protein attenuates the ER-to-cytosol transport of CTA1, indicating that Derlins-1 facilitates the retro-translocation of CT. Expand
Ganglioside Structure Dictates Signal Transduction by Cholera Toxin and Association with Caveolae-like Membrane Domains in Polarized Epithelia
Analysis of CT and LTIIb chimeric toxins confirmed that toxin-induced signal transduction depended critically on the specificity of ganglioside structure, and likely depends on coupling CT with caveolae or Caveolae-related membrane domains. Expand