Evidence map›Paper›PMID 13679513›Full record

ArticleMolecular biology of the cell2003

Gangliosides that associate with lipid rafts mediate transport of cholera and related toxins from the plasma membrane to endoplasmic reticulm.

Yukako Fujinaga, Anne A Wolf, Chiara Rodighiero, Heidi Wheeler, Billy Tsai, Larry Allen, Michael G Jobling, Tom Rapoport, Randall K Holmes, Wayne I Lencer

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 108 papers.

0numbers the graph read from it
0cells of the map it votes in
108citing papers in PubMed
6.8field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

108 citing papers in PubMed, 230 citations in OpenAlex.

  1. Cholera toxin as a model ABArchives of toxicology · 2026
    Review
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  13. Lipid Raft Association Stabilizes VEGF Receptor 2 in Endothelial Cells.International journal of molecular sciences · 2021
    Article
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  15. Article
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48 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 2 countries.

Yukako FujinagaGI Cell Biology, Children's Hospital and Harvard Medical School, Boston, Massachusetts 02115, USA.
Anne A Wolf
Chiara Rodighiero
Heidi Wheeler
Billy Tsai
Larry Allen
Michael G Jobling
Tom Rapoport
Randall K Holmes
Wayne I Lencer
Boston Children's Hospital · USHarvard University · USUniversity of Colorado Health · US

Funding

STRUCTURE-FUNCTION RELATIONSHIPS IN THE ALIMENTARY TRACTP30DK034854 · NIDDK · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WAYNE I LENCER · 1986 to 2026
$32.4M
Mechanism of action for the epithelial-specific ER stress sensor IRE1β in regulating intestinal homeostasis and host defenseR01DK048106 · NIDDK · CHILDREN'S HOSPITAL BOSTON · PI WAYNE I LENCER · 1993 to 2026
$9.6M
Intestinal Disease-enterocyte toxin interactionR37DK048106 · NIDDK · BOSTON CHILDREN'S HOSPITAL · PI LENCER, WAYNE I · 2011 to 2020
$7.0M
GENETIC ANALYSIS OF CHOLERA TOXIN STRUCTURE AND FUNCTIONR01AI031940 · NIAID · UNIVERSITY OF COLORADO DENVER · PI HOLMES, RANDALL K · 1992 to 2011
$5.9M
CRYPTDIN EFFECTS ON CRYPT EPITHELIAR01DK057827 · NIDDK · UNIVERSITY OF CHICAGO · PI LENCER, WAYNE · 2000 to 2004
$1.0M
NIAID NIH HHS AI31940NIAID NIH HHS R01 AI031940NIDDK NIH HHS DK34854NIDDK NIH HHS DK48106NIDDK NIH HHS DK57827NIDDK NIH HHS P30 DK034854NIDDK NIH HHS R01 DK048106NIDDK NIH HHS R01 DK057827NIDDK NIH HHS R37 DK048106
6 · The paper itself

Abstract

Cholera toxin (CT) travels from the plasma membrane of intestinal cells to the endoplasmic reticulum (ER) where a portion of the A-subunit, the A1 chain, crosses the membrane into the cytosol to cause disease. A related toxin, LTIIb, binds to intestinal cells but does not cause toxicity. Here, we show that the B-subunit of CT serves as a carrier for the A-subunit to the ER where disassembly occurs. The B-subunit binds to gangliosides in lipid rafts and travels with the ganglioside to the ER. In many cells, LTIIb follows a similar pathway, but in human intestinal cells it binds to a ganglioside that fails to associate with lipid rafts and it is sorted away from the retrograde pathway to the ER. Our results explain why LTIIb does not cause disease in humans and suggest that gangliosides with high affinity for lipid rafts may provide a general vehicle for the transport of toxins to the ER.

Indexed as

AnimalsBacterial ToxinsBiological TransportCells, CulturedCholera ToxinCloning, MolecularEndocytosisEndoplasmic ReticulumEpithelial CellsGangliosidesGolgi ApparatusHumansIntestinal MucosaMembrane MicrodomainsProtein BindingProtein SubunitsBacterial ToxinsCholera ToxinGangliosidesProtein Subunits

Identifiers

PMID13679513
PMCPMC284783
OpenAlexW2104596749

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.