Evidence map›Paper›PMID 17651732›Full record

ArticleExperimental cell research2007

Membrane fusion by VAMP3 and plasma membrane t-SNAREs.

Chuan Hu, Deborah Hardee, Fred Minnear

Open access · greenAbstract read
In one paragraph

Article in Experimental cell research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
0.4field-weighted citation impact, top 40% 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

26 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Article
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  4. Vamp3/syntaxin 4 mediates the basolateral membrane fusion of TfR transcytosis across the BBB and is exploited by pathogenicProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Type III Secretion inMicrobiology and molecular biology reviews : MMBR · 2023
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. The function of VAMP2 in mediating membrane fusion: An overview.Frontiers in molecular neuroscience · 2022
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Bovine Herpesvirus 1 UJournal of virology · 2018
    Article
  19. Brain Delivery of Multifunctional Dendrimer Protein Bioconjugates.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2018
    Article
  20. Article
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

3 authors at 2 institutions in 1 country.

Chuan HuDepartment of Physiology and Pharmacology, West Virginia University Health Sciences Center, Morgantown, WV 26506, USA. chuan.hu@louisville.edu
Deborah Hardee
Fred Minnear
West Virginia University · USUniversity of Louisville · US

Funding

Adherens Junction Integrity and Barrier FunctionR01HL068079 · NHLBI · WEST VIRGINIA UNIVERSITY · PI MINNEAR, FRED L · 2002 to 2005
$1.1M
NHLBI NIH HHS HL-68079NHLBI NIH HHS R01 HL068079
6 · The paper itself

Abstract

Pairing of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins on vesicles (v-SNAREs) and SNARE proteins on target membranes (t-SNAREs) mediates intracellular membrane fusion. VAMP3/cellubrevin is a v-SNARE that resides in recycling endosomes and endosome-derived transport vesicles. VAMP3 has been implicated in recycling of transferrin receptors, secretion of alpha-granules in platelets, and membrane trafficking during cell migration. Using a cell fusion assay, we examined membrane fusion capacity of the ternary complexes formed by VAMP3 and plasma membrane t-SNAREs syntaxin1, syntaxin4, SNAP-23 and SNAP-25. VAMP3 forms fusogenic pairing with t-SNARE complexes syntaxin1/SNAP-25, syntaxin1/SNAP-23 and syntaxin4/SNAP-25, but not with syntaxin4/SNAP-23. Deletion of the N-terminal domain of syntaxin4 enhanced membrane fusion more than two fold, indicating that the N-terminal domain negatively regulates membrane fusion. Differential membrane fusion capacities of the ternary v-/t-SNARE complexes suggest that transport vesicles containing VAMP3 have distinct membrane fusion kinetics with domains of the plasma membrane that present different t-SNARE proteins.

Indexed as

AnimalsCell MembraneChlorocebus aethiopsCloning, MolecularCOS CellsMembrane FusionMiceMutationQa-SNARE ProteinsQb-SNARE ProteinsQc-SNARE ProteinsSynaptosomal-Associated Protein 25Vesicle-Associated Membrane Protein 3Qa-SNARE ProteinsQb-SNARE ProteinsQc-SNARE ProteinsSnap23 protein, mouseSynaptosomal-Associated Protein 25Vesicle-Associated Membrane Protein 3vesicle-associated membrane protein 3, mouse

Identifiers

PMID17651732
PMCPMC2696983
OpenAlexW2023338791

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.