Evidence map›Paper›PMID 19258315›Full record

ArticleThe Journal of biological chemistry2009

Is assembly of the SNARE complex enough to fuel membrane fusion?

Katrin Wiederhold, Dirk Fasshauer

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
–field-weighted citation impact
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

47 citing papers in PubMed.

  1. Review
  2. Intermediate steps in the formation of neuronal SNARE complexes.The Journal of biological chemistry · 2024
    Article
  3. Mechanisms of SNARE proteins in membrane fusion.Nature reviews. Molecular cell biology · 2024
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. The control of release probability at nerve terminals.Nature reviews. Neuroscience · 2019
    Review
  9. v-SNARE function in chromaffin cells.Pflugers Archiv : European journal of physiology · 2018
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Energetics, kinetics, and pathway of SNARE folding and assembly revealed by optical tweezers.Protein science : a publication of the Protein Society · 2017
    Review
  15. Article
  16. Article
  17. Review
  18. Kinetic barriers to SNAREpin assembly in the regulation of membrane docking/priming and fusion.Proceedings of the National Academy of Sciences of the United States of America · 2016
    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

2 authors.

Katrin WiederholdResearch Group Structural Biochemistry, Department of Neurobiology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, Göttingen, Germany.
Dirk Fasshauer

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The three key players in the exocytotic release of neurotransmitters from synaptic vesicles are the SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins synaptobrevin 2, syntaxin 1a, and SNAP-25. Their assembly into a tight four-helix bundle complex is thought to pull the two membranes into close proximity. It is debated, however, whether the energy generated suffices for membrane fusion. Here, we have determined the thermodynamic properties of the individual SNARE assembly steps by isothermal titration calorimetry. We found extremely large favorable enthalpy changes counterbalanced by positive entropy changes, reflecting the major conformational changes upon assembly. To circumvent the fact that ternary complex formation is essentially irreversible, we used a stabilized syntaxin-SNAP-25 heterodimer to study synaptobrevin binding. This strategy revealed that the N-terminal synaptobrevin coil binds reversibly with nanomolar affinity. This suggests that individual, membrane-bridging SNARE complexes can provide much less pulling force than previously claimed.

Indexed as

CalorimetryCircular DichroismDimerizationHumansLiposomesMembrane FusionProtein ConformationQa-SNARE ProteinsR-SNARE ProteinsSNARE ProteinsSynaptic VesiclesSynaptosomal-Associated Protein 25LiposomesQa-SNARE ProteinsR-SNARE ProteinsSNAP25 protein, humanSNARE ProteinsSynaptosomal-Associated Protein 25

Identifiers

PMID19258315
PMCPMC2676046

What OpenQuestion holds

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Registered trials

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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.