Evidence map›Paper›PMID 16418536›Full record

ArticleThe Journal of cell biology2006

Structural transitions in the synaptic SNARE complex during Ca2+-triggered exocytosis.

Xue Han, Meyer B Jackson

Open access · greenAbstract 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 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

23 citing papers in PubMed, 58 citations in OpenAlex.

  1. Fusion Pores as Regulators of Quantal Size and Cellular Physiology.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  2. Article
  3. SNARE Proteins in Synaptic Vesicle Fusion.Advances in neurobiology · 2023
    Article
  4. Article
  5. Article
  6. Article
  7. The Phosphoprotein Synapsin Ia Regulates the Kinetics of Dense-Core Vesicle Release.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. The SNARE complex in neuronal and sensory cells.Molecular and cellular neurosciences · 2012
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. The fusion pores of Ca2+ -triggered exocytosis.Nature structural & molecular biology · 2008
    Review
  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 at 1 institution in 1 country.

Xue HanDepartment of Physiology, University of Wisconsin Medical School, Madison, WI 53706, USA.
Meyer B Jackson
University of Wisconsin–Madison · US

Funding

Single-Channel Studies of the Fusion PoreR01NS044057 · NINDS · UNIVERSITY OF WISCONSIN-MADISON · PI JACKSON, MEYER B. · 2002 to 2022
$5.7M
MEMBRANE EXCITABILITY AND SECRETION FROM NERVE ENDINGSR37NS030016 · NINDS · UNIVERSITY OF WISCONSIN-MADISON · PI JACKSON, MEYER B. · 2001 to 2007
$2.2M
MEMBRANE EXCITABILITY AND SECRETION FROM NERVE ENDINGSR01NS030016 · NINDS · UNIVERSITY OF WISCONSIN MADISON · PI JACKSON, MEYER B. · 1992 to 2000
$159k
NINDS NIH HHS NS30016NINDS NIH HHS NS44057NINDS NIH HHS R01 NS030016NINDS NIH HHS R01 NS044057NINDS NIH HHS R37 NS030016
6 · The paper itself

Abstract

The synaptic SNARE complex is a highly stable four-helix bundle that links the vesicle and plasma membranes and plays an essential role in the Ca(2+)-triggered release of neurotransmitters and hormones. An understanding has yet to be achieved of how this complex assembles and undergoes structural transitions during exocytosis. To investigate this question, we have mutated residues within the hydrophobic core of the SNARE complex along the entire length of all four chains and examined the consequences using amperometry to measure fusion pore opening and dilation. Mutations throughout the SNARE complex reduced two distinct rate processes before fusion pore opening to different degrees. These results suggest that two distinct, fully assembled conformations of the SNARE complex drive transitions leading to open fusion pores. In contrast, a smaller number of mutations that were scattered through the SNARE complex but were somewhat concentrated in the membrane-distal half stabilized open fusion pores. These results suggest that a structural transition within a partially disassembled complex drives the dilation of open fusion pores. The dependence of these three rate processes on position within the SNARE complex does not support vectorial SNARE complex zipping during exocytosis.

Indexed as

Amino Acid SequenceAnimalsCalciumExocytosisMembrane FusionModels, MolecularMolecular Sequence DataMultiprotein ComplexesMutationPC12 CellsRatsSequence AlignmentSNARE ProteinsSoluble N-Ethylmaleimide-Sensitive Factor Attachment ProteinsSynapsesCalciumMultiprotein ComplexesSNARE ProteinsSoluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins

Identifiers

PMID16418536
PMCPMC2063557
OpenAlexW2104374433

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.