Evidence map›Paper›PMID 16195346›Full record

ArticleMolecular biology of the cell2005

Alternative splicing of SNAP-25 regulates secretion through nonconservative substitutions in the SNARE domain.

Gábor Nagy, Ira Milosevic, Dirk Fasshauer, E Matthias Müller, Bert L de Groot, Thorsten Lang, Michael C Wilson, Jakob B Sørensen

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed, 1 pooled it
2.5field-weighted citation impact, top 12% 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

36 citing papers in PubMed, 1 synthesis or guideline pooled it, 78 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Isoswitching drives the aging process in human brains.bioRxiv : the preprint server for biology · 2025
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. SNARE complex in developmental psychiatry: neurotransmitter exocytosis and beyond.Journal of neural transmission (Vienna, Austria : 1996) · 2016
    Review
  12. Article
  13. Article
  14. Synaptotagmin interaction with SNAP-25 governs vesicle docking, priming, and fusion triggering.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013
    Article
  15. Review
  16. Review
  17. SNARE requirements en route to exocytosis: from many to few.Journal of molecular neuroscience : MN · 2012
    Review
  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

8 authors at 2 institutions in 2 countries.

Gábor NagyDepartment of Membrane Biophysics, Max-Planck-Institute for Biophysical Chemistry, 37077 Göttingen, Germany.
Ira Milosevic
Dirk Fasshauer
E Matthias Müller
Bert L de Groot
Thorsten Lang
Michael C Wilson
Jakob B Sørensen
Max Planck Institute for Biophysical Chemistry · DEUniversity of New Mexico · US

Funding

SNAP-25 EXPRESSION AND HYPERACTIVITY IN COLOBOMA MICER01MH048989 · NIMH · UNIVERSITY OF NEW MEXICO · PI WILSON, MICHAEL COLIN · 1992 to 2008
$2.7M
NIMH NIH HHS MH-48989NIMH NIH HHS R01 MH048989
6 · The paper itself

Abstract

The essential membrane fusion apparatus in mammalian cells, the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex, consists of four alpha-helices formed by three proteins: SNAP-25, syntaxin 1, and synaptobrevin 2. SNAP-25 contributes two helices to the complex and is targeted to the plasma membrane by palmitoylation of four cysteines in the linker region. It is alternatively spliced into two forms, SNAP-25a and SNAP-25b, differing by nine amino acids substitutions. When expressed in chromaffin cells from SNAP-25 null mice, the isoforms support different levels of secretion. Here, we investigated the basis of that different secretory phenotype. We found that two nonconservative substitutions in the N-terminal SNARE domain and not the different localization of one palmitoylated cysteine cause the functional difference between the isoforms. Biochemical and molecular dynamic simulation experiments revealed that the two substitutions do not regulate secretion by affecting the property of SNARE complex itself, but rather make the SNAP-25b-containing SNARE complex more available for the interaction with accessory factor(s).

Indexed as

Alternative SplicingAmino Acid SequenceAmino Acid SubstitutionAnimalsChromaffin CellsCircular DichroismComputer SimulationExonsMiceMice, KnockoutMolecular Sequence DataSNARE ProteinsSynaptosomal-Associated Protein 25SNARE ProteinsSynaptosomal-Associated Protein 25

Identifiers

PMID16195346
PMCPMC1289412
OpenAlexW2143320037

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.