Ganglioside GM1-mediated Transcytosis of Cholera Toxin Bypasses the Retrograde Pathway and Depends on the Structure of the Ceramide Domain-Reference-Cited by-同舟云学术

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Ganglioside GM1-mediated Transcytosis of Cholera Toxin Bypasses the Retrograde Pathway and Depends on the Structure of the Ceramide Domain

Published:2013-09 Issue:36 Volume:288 Page:25804-25809
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Saslowsky David E.,te Welscher Yvonne M.,Chinnapen Daniel J.-F.,Wagner Jessica S.,Wan Joy,Kern Eli,Lencer Wayne I.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference21 articles.

1. Lipid sorting by ceramide structure from plasma membrane to ER for the cholera toxin receptor ganglioside GM1;Chinnapen;Dev. Cell,2012

2. A single native ganglioside GM1-binding site is sufficient for cholera toxin to bind to cells and complete the intoxication pathway;Jobling;mBio,2012

3. Attenuated endocytosis and toxicity of a mutant cholera toxin with decreased ability to cluster ganglioside GM1 molecules;Wolf;Infect. Immun,2008

4. Transcytosis of cholera toxin subunits across model human intestinal epithelia;Lencer;Proc. Natl. Acad. Sci. U.S.A,1995

5. Targeting of cholera toxin and E. coli heat labile toxin in polarized epithelia. Role of C-terminal KDEL;Lencer;J. Cell Biol,1995

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