Cholera Toxin: An Intracellular Journey into the Cytosol by Way of the Endoplasmic Reticulum
AbstractCholera toxin (CT), an AB5-subunit toxin, enters host cells by binding the ganglioside GM1 at the plasma membrane (PM) and travels retrograde through the trans-Golgi Network into the endoplasmic reticulum (ER). In the ER, a portion of CT, the enzymatic A1-chain, is unfolded by protein disulfide isomerase and retro-translocated to the cytosol by hijacking components of the ER associated degradation pathway for misfolded proteins. After crossing the ER membrane, the A1-chain refolds in the cytosol and escapes rapid degradation by the proteasome to induce disease by ADP-ribosylating the large G-protein Gs and activating adenylyl cyclase. Here, we review the mechanisms of toxin trafficking by GM1 and retro-translocation of the A1-chain to the cytosol.
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Wernick, N.L.B.; Chinnapen, D.-F.; Cho, J.A.; Lencer, W.I. Cholera Toxin: An Intracellular Journey into the Cytosol by Way of the Endoplasmic Reticulum. Toxins 2010, 2, 310-325.
Wernick NLB, Chinnapen D-F, Cho JA, Lencer WI. Cholera Toxin: An Intracellular Journey into the Cytosol by Way of the Endoplasmic Reticulum. Toxins. 2010; 2(3):310-325.Chicago/Turabian Style
Wernick, Naomi L. B.; Chinnapen, Daniel J.-F.; Cho, Jin Ah; Lencer, Wayne I. 2010. "Cholera Toxin: An Intracellular Journey into the Cytosol by Way of the Endoplasmic Reticulum." Toxins 2, no. 3: 310-325.