Evidence map›Paper›PMID 9487128›Full record

ArticleMolecular biology of the cell1998

SNAP-25 palmitoylation and plasma membrane targeting require a functional secretory pathway.

S Gonzalo, M E Linder

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

78 citing papers in PubMed, 196 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. SNARE Proteins in Synaptic Vesicle Fusion.Advances in neurobiology · 2023
    Article
  6. A SNARE-like protein fromFrontiers in plant science · 2023
    Article
  7. PI(4,5)P2: signaling the plasma membrane.The Biochemical journal · 2022
    Article
  8. Review
  9. Article
  10. Fluid markers of synapse degeneration in synucleinopathies.Journal of neural transmission (Vienna, Austria : 1996) · 2022
    Review
  11. Review
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. RPE65 Palmitoylation: A Tale of Lipid Posttranslational Modification.Advances in experimental medicine and biology · 2019
    Review

18 more citing papers are in PubMed but not listed here.

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.

S GonzaloDepartment of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
M E Linder
Washington University in St. Louis · US

Funding

MOLECULAR, BIOCHEMICAL, AND PHYSIOLOGICAL PHARMACOLOGYT32GM007805 · NIGMS · WASHINGTON UNIVERSITY · PI RUSSELL, JOHN H · 1985 to 1995
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NIGMS NIH HHS 5T32GM07805NIGMS NIH HHS GM50556
6 · The paper itself

Abstract

Synaptosomal-associated protein of 25 kDa (SNAP-25) is a palmitoylated membrane protein essential for neurotransmitter release from synaptic terminals. We used neuronal cell lines to study the biosynthesis and posttranslational processing of SNAP-25 to investigate how palmitoylation contributes to the subcellular localization of the protein. SNAP-25 was synthesized as a soluble protein that underwent palmitoylation approximately 20 min after synthesis. Palmitoylation of the protein coincided with its stable membrane association. Treatment of cells with brefeldin A or other disrupters of transport inhibited palmitoylation of newly synthesized SNAP-25 and abolished membrane association. These results demonstrate that the processing of SNAP-25 and its targeting to the plasma membrane depend on an intact transport mechanism along the exocytic pathway. The kinetics of SNAP-25 palmitoylation and membrane association and the sensitivity of these parameters to brefeldin A suggest a novel trafficking pathway for targeting proteins to the plasma membrane. In vitro, SNAP-25 stably associated with membranes was not released from the membrane after chemical deacylation. We propose that palmitoylation of SNAP-25 is required for initial membrane targeting of the protein but that other interactions can maintain membrane association in the absence of fatty acylation.

Indexed as

Membrane ProteinsAcylationAnimalsBiological Transport, ActiveBrefeldin ACell LineCell MembraneCyclopentanesGAP-43 ProteinGTP-Binding ProteinsKineticsNerve Tissue ProteinsNeurotransmitter AgentsPalmitic AcidsPC12 CellsPresynaptic TerminalsBrefeldin ACyclopentanesGAP-43 ProteinGTP-Binding ProteinsMembrane ProteinsNerve Tissue ProteinsNeurotransmitter AgentsPalmitic AcidsProtein Synthesis InhibitorsSnap25 protein, ratSynaptosomal-Associated Protein 25

Identifiers

PMID9487128
PMCPMC25287
OpenAlexW2145075118

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.