Evidence map›Paper›PMID 17159904›Full record

ArticleThe EMBO journal2007

Early endosomal SNAREs form a structurally conserved SNARE complex and fuse liposomes with multiple topologies.

Daniel Zwilling, Anna Cypionka, Wiebke H Pohl, Dirk Fasshauer, Peter J Walla, Markus C Wahl, Reinhard Jahn

Abstract read
In one paragraph

Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

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

48 citing papers in PubMed.

  1. Article
  2. Article
  3. Mechanisms of SNARE proteins in membrane fusion.Nature reviews. Molecular cell biology · 2024
    Review
  4. Article
  5. Review
  6. Schizophrenia-Linked Protein tSNARE1 Regulates Endosomal Trafficking in Cortical Neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
  7. Article
  8. Selected tools to visualize membrane interactions.European biophysics journal : EBJ · 2021
    Review
  9. Decoding three distinct states of the Syntaxin17 SNARE motif in mediating autophagosome-lysosome fusion.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  10. Article
  11. Article
  12. Article
  13. Single-Molecule Optical Tweezers Study of Regulated SNARE Assembly.Methods in molecular biology (Clifton, N.J.) · 2019
    Article
  14. Article
  15. Probing and manipulating intracellular membrane traffic by microinjection of artificial vesicles.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  16. SNARE zippering.Bioscience reports · 2016
    Review
  17. Article
  18. Article
  19. 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

7 authors.

Daniel ZwillingDepartment of Neurobiology, Max-Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Anna Cypionka
Wiebke H Pohl
Dirk Fasshauer
Peter J Walla
Markus C Wahl
Reinhard Jahn

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SNARE proteins mediate membrane fusion in eukaryotic cells. They contain conserved SNARE motifs that are usually located adjacent to a C-terminal transmembrane domain. SNARE motifs spontaneously assemble into four helix bundles, with each helix belonging to a different subfamily. Liposomes containing SNAREs spontaneously fuse with each other, but it is debated how the SNAREs are distributed between the membranes. Here, we report that the SNAREs mediating homotypic fusion of early endosomes fuse liposomes in five out of seven possible combinations, in contrast to previously studied SNAREs involved in heterotypic fusion events. The crystal structure of the early endosomal SNARE complex resembles that of the neuronal and late endosomal complexes, but differs in surface side-chain interactions. We conclude that homotypic fusion reactions may proceed with multiple SNARE topologies, suggesting that the conserved SNARE structure allows for flexibility in the initial interactions needed for fusion.

Indexed as

Amino Acid SequenceAnimalsCircular DichroismCrystallography, X-RayEndosomesLiposomesMiceModels, MolecularMolecular Sequence DataProtein BindingProtein ConformationProtein Structure, TertiarySequence Homology, Amino AcidSNARE ProteinsSpectrometry, FluorescenceLiposomesSNARE Proteins

Identifiers

PMID17159904
PMCPMC1782365

What OpenQuestion holds

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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.