Evidence map›Paper›PMID 16880274›Full record

ArticleThe Journal of cell biology2006

Tetanus toxin is internalized by a sequential clathrin-dependent mechanism initiated within lipid microdomains and independent of epsin1.

Katrin Deinhardt, Otto Berninghausen, Hugh J Willison, Colin R Hopkins, Giampietro Schiavo

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

56 citing papers in PubMed, 130 citations in OpenAlex.

  1. Review
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  11. Tetanus in animals.Journal of veterinary diagnostic investigation : official publication of the American Association of Veterinary Laboratory Diagnosticians, Inc · 2020
    Review
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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

5 authors at 3 institutions in 1 country.

Katrin DeinhardtMolecular Neuropathobiology Laboratory, Cancer Research UK London Research Institute, London WC2A 3PX, England, UK.
Otto Berninghausen
Hugh J Willison
Colin R Hopkins
Giampietro Schiavo
Cancer Research UK · GBImperial College London · GBSouthern General Hospital · GB

Funding

Wellcome TrustWellcome Trust 060349
6 · The paper itself

Abstract

Ligand-receptor complexes are internalized by a variety of endocytic mechanisms. Some are initiated within clathrin-coated membranes, whereas others involve lipid microdomains of the plasma membrane. In neurons, where alternative targeting to short- or long-range trafficking routes underpins the differential processing of synaptic vesicle components and neurotrophin receptors, the mechanism giving access to the axonal retrograde pathway remains unknown. To investigate this sorting process, we examined the internalization of a tetanus neurotoxin fragment (TeNT HC), which shares axonal carriers with neurotrophins and their receptors. Previous studies have shown that the TeNT HC receptor, which comprises polysialogangliosides, resides in lipid microdomains. We demonstrate that TeNT HC internalization also relies on a specialized clathrin-mediated pathway, which is independent of synaptic vesicle recycling. Moreover, unlike transferrin uptake, this AP-2-dependent process is independent of epsin1. These findings identify a pathway for TeNT, beginning with the binding to a lipid raft component (GD1b) and followed by dissociation from GD1b as the toxin internalizes via a clathrin-mediated mechanism using a specific subset of adaptor proteins.

Indexed as

Adaptor Protein Complex SubunitsAdaptor Proteins, Vesicular TransportAnimalsCells, CulturedClathrinCoated Pits, Cell-MembraneDynaminsEndocytosisExocytosisGangliosidesMembrane MicrodomainsModels, BiologicalMotor NeuronsPeptide FragmentsPresynaptic TerminalsProtein TransportAdaptor Protein Complex SubunitsAdaptor Proteins, Vesicular TransportClathrinDynaminsepsinganglioside, GD1bGangliosidesPeptide FragmentsTetanus Toxintetanus toxin fragment C

Identifiers

PMID16880274
PMCPMC2064241
OpenAlexW1982712294

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.