Evidence map›Paper›PMID 9618556›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1998

Modulation of an early step in the secretory machinery in hippocampal nerve terminals.

L E Trudeau, Y Fang, P G Haydon

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed, 1 pooled it
2.2field-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

35 citing papers in PubMed, 1 synthesis or guideline pooled it, 81 citations in OpenAlex.

  1. Pooled it
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  7. 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
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  15. Differential abilities of SNAP-25 homologs to support neuronal function.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2007
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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

3 authors at 1 institution in 2 countries.

L E TrudeauLaboratory of Cellular Signaling, Department of Zoology and Genetics, Iowa State University, Ames, IA 50011, USA. Trudeal@ere.umontreal.ca
Y Fang
P G Haydon
Iowa State University · US

Funding

THE REGULATION OF SYNAPTOGENESISR01NS024233 · NINDS · IOWA STATE UNIVERSITY · PI HAYDON, PHILIP G · 1987 to 1999
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CALCIUM CHANNELS &G-PROTEINS IN SYNAPTIC TRANSMISSIONR01NS026650 · NINDS · IOWA STATE UNIVERSITY · PI HAYDON, PHILIP G · 1989 to 1996
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NINDS NIH HHS NS24233NINDS NIH HHS NS26650
6 · The paper itself

Abstract

In hippocampal neurons, neurotransmitter release can be regulated by protein kinase A (PKA) through a direct action on the secretory machinery. To identify the site of PKA modulation, we have taken advantage of the ability of the neurotoxin Botulinum A to cleave the synaptic protein SNAP-25. Cleavage of this protein decreases the Ca2+ responsiveness of the secretory machinery by partially uncoupling Ca2+-sensing from fusion per se. This is expressed as a shift toward higher Ca2+ levels of the Ca2+ to neurotransmitter release relationship and as a perturbation of synaptic delay under conditions where secretion induced by the Ca2+-independent secretagogue ruthenium red is unimpaired. We find that SNAP-25 cleavage also perturbs PKA-dependent modulation of secretion; facilitation of ruthenium red-evoked neurotransmitter release by the adenylyl cyclase activator forskolin is blocked completely after Botulinum toxin A action. Together with our observation that forskolin modifies the Ca2+ to neurotransmitter release relationship, our results suggest that SNAP-25 acts as a functional linker between Ca2+ detection and fusion and that PKA modulates an early step in the secretory machinery related to calcium sensing to facilitate synaptic transmission.

Indexed as

Membrane ProteinsAnimalsBotulinum Toxins, Type ACalciumCyclic AMP-Dependent Protein KinasesElectrophysiologyHippocampusNerve Tissue ProteinsNeuromuscular AgentsRatsSynapsesSynaptic TransmissionSynaptosomal-Associated Protein 25Botulinum Toxins, Type ACalciumCyclic AMP-Dependent Protein KinasesMembrane ProteinsNerve Tissue ProteinsNeuromuscular AgentsSnap25 protein, ratSynaptosomal-Associated Protein 25

Identifiers

PMID9618556
PMCPMC22774
OpenAlexW2138533858

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.