ArticleThe Journal of cell biology1998
Ganglioside structure dictates signal transduction by cholera toxin and association with caveolae-like membrane domains in polarized epithelia.
Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
64 citing papers in PubMed, 225 citations in OpenAlex.
- Membrane lipid remodeling eradicates Helicobacter pylori by manipulating the cholesteryl 6'-acylglucoside biosynthesis.Journal of biomedical science · 2024Article
- The diverse landscape of AB5-type toxins.Engineering microbiology · 2023Review
- Bacterial toxins and heart function: heat-labileBiophysical reviews · 2023Article
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- Chemogenetic inhibition of TrkB signalling reduces phrenic motor neuron survival and size.Molecular and cellular neurosciences · 2023Article
- Aging affects the number and morphological heterogeneity of rat phrenic motor neurons and phrenic motor axons.Physiological reports · 2023Article
- Cell-Free Systems Enable the Production of ABToxins · 2022Article
- Cholera Toxin as a Probe for Membrane Biology.Toxins · 2021Review
- Crystal structures of cholera toxin in complex with fucosylated receptors point to importance of secondary binding site.Scientific reports · 2019Article
- Protein Toxins That Utilize Gangliosides as Host Receptors.Progress in molecular biology and translational science · 2018Review
- Membrane lipid rafts and neurobiology: age-related changes in membrane lipids and loss of neuronal function.The Journal of physiology · 2016Review
- Ouabain Modulates the Lipid Composition of Hippocampal Plasma Membranes from Rats with LPS-induced Neuroinflammation.The Journal of membrane biology · 2015Article
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- Pathogenesis of human enterovirulent bacteria: lessons from cultured, fully differentiated human colon cancer cell lines.Microbiology and molecular biology reviews : MMBR · 2013Review
- Lipid sorting by ceramide structure from plasma membrane to ER for the cholera toxin receptor ganglioside GM1.Developmental cell · 2012Article
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- Involvement of lipid rafts in adhesion-induced activation of Met and EGFR.Journal of biomedical science · 2011Article
- Src family kinases mediate epidermal growth factor receptor signaling from lipid rafts in breast cancer cells.Cancer biology & therapy · 2011Article
4 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
Abstract
In polarized cells, signal transduction by cholera toxin (CT) requires apical endocytosis and retrograde transport into Golgi cisternae and perhaps ER (Lencer, W.I., C. Constable, S. Moe, M. Jobling, H.M. Webb, S. Ruston, J.L. Madara, T. Hirst, and R. Holmes. 1995. J. Cell Biol. 131:951-962). In this study, we tested whether CT's apical membrane receptor ganglioside GM1 acts specifically in toxin action. To do so, we used CT and the related Escherichia coli heat-labile type II enterotoxin LTIIb. CT and LTIIb distinguish between gangliosides GM1 and GD1a at the cell surface by virtue of their dissimilar receptor-binding B subunits. The enzymatically active A subunits, however, are homologous. While both toxins bound specifically to human intestinal T84 cells (Kd approximately 5 nM), only CT elicited a cAMP-dependent Cl- secretory response. LTIIb, however, was more potent than CT in eliciting a cAMP-dependent response from mouse Y1 adrenal cells (toxic dose 10 vs. 300 pg/well). In T84 cells, CT fractionated with caveolae-like detergent-insoluble membranes, but LTIIb did not. To investigate further the relationship between the specificity of ganglioside binding and partitioning into detergent-insoluble membranes and signal transduction, CT and LTIIb chimeric toxins were prepared. Analysis of these chimeric toxins confirmed that toxin-induced signal transduction depended critically on the specificity of ganglioside structure. The mechanism(s) by which ganglioside GM1 functions in signal transduction likely depends on coupling CT with caveolae or caveolae-related membrane domains.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.